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Rhodopsin Structure
Published by Anonymous on 2007/9/30 (1542 reads)
1: Physiol Rev. 2007 Apr;87(2):565-92.


The angiotensin II AT1 receptor structure-activity correlations in the light of rhodopsin structure.

Oliveira L, Costa-Neto CM, Nakaie CR, Schreier S, Shimuta SI, Paiva AC.

Department of Biophysics, Escola Paulista de Medicina, Federal University of São Paulo, Brazil. laerte@biofls.epm.br

The most prevalent physiological effects of ANG II, the main product of the renin-angiotensin system, are mediated by the AT1 receptor, a rhodopsin-like AGPCR. Numerous studies of the cardiovascular effects of synthetic peptide analogs allowed a detailed mapping of ANG II's structural requirements for receptor binding and activation, which were complemented by site-directed mutagenesis studies on the AT1 receptor to investigate the role of its structure in ligand binding, signal transduction, phosphorylation, binding to arrestins, internalization, desensitization, tachyphylaxis, and other properties. The knowledge of the high-resolution structure of rhodopsin allowed homology modeling of the AT1 receptor. The models thus built and mutagenesis data indicate that physiological (agonist binding) or constitutive (mutated receptor) activation may involve different degrees of expansion of the receptor's central cavity. Residues in ANG II structure seem to control these conformational changes and to dictate the type of cytosolic event elicited during the activation. 1) Agonist aromatic residues (Phe8 and Tyr4) favor the coupling to G protein, and 2) absence of these residues can favor a mechanism leading directly to receptor internalization via phosphorylation by specific kinases of the receptor's COOH-terminal Ser and Thr residues, arrestin binding, and clathrin-dependent coated-pit vesicles. On the other hand, the NH2-terminal residues of the agonists ANG II and [Sar1]-ANG II were found to bind by two distinct modes to the AT1 receptor extracellular site flanked by the COOH-terminal segments of the EC-3 loop and the NH2-terminal domain. Since the [Sar1]-ligand is the most potent molecule to trigger tachyphylaxis in AT1 receptors, it was suggested that its corresponding binding mode might be associated with this special condition of receptors.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 17429042 [PubMed - indexed for MEDLINE]

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2: J Biol Chem. 2007 Mar 30;282(13):9297-301. Epub 2007 Feb 8.


Visual rhodopsin sees the light: structure and mechanism of G protein signaling.

Ridge KD, Palczewski K.

Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center, Houston, Texas 77030, USA. Kevin.D.Ridge@uth.tmc.edu

The availability of crystal structures for the dark, inactive, and several light-activated photointermediate states of vertebrate visual rhodopsin has provided important mechanistic and energetic insights into the transformations underlying agonist-dependent activation of this and other G protein-coupled receptors (GPCRs). The high natural abundance of rhodopsin in the vertebrate retina, together with its specific localization to the disk membranes of the rod cell, has also enabled direct imaging of rhodopsin in its native environment. These advances have provided compelling evidence that rhodopsin, like many other GPCRs, forms highly organized oligomeric structures that, in all likelihood, are important for receptor biosynthesis, optimal activation, and signaling.

Publication Types:
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

PMID: 17289671 [PubMed - indexed for MEDLINE]

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3: Chembiochem. 2007 Jan 2;8(1):19-24.


The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors.

Pardo L, Deupi X, Dölker N, López-Rodríguez ML, Campillo M.

Laboratori de Medicina Computacional, Unitat de Bioestadística, Facultat de Medicina, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain. Leonardo.Pardo@uab.es

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 17173267 [PubMed - indexed for MEDLINE]

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4: Vision Res. 2006 Dec;46(27):4434-41. Epub 2006 Sep 26.


Oligomeric structure of the alpha1b-adrenoceptor: comparisons with rhodopsin.

Milligan G, Pediani JD, Canals M, Lopez-Gimenez JF.

Molecular Pharmacology Group, Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, UK. g.milligan@bio.gla.ac.uk

The structural basis of the quaternary organization of rhodopsin has recently been explored and modeled. Because information obtained from studying rhodopsin has frequently been directly applicable to other G protein-coupled receptors we wished to ascertain if dimeric and/or oligomeric forms of the alpha(1b)-adrenoceptor could be observed and if so whether rhodopsin might provide insights into the quaternary structure of this receptor. Co-immunoprecipitation and both conventional and time-resolved fluorescence resonance energy transfer studies demonstrated quaternary structure of the alpha(1b)-adrenoceptor and, in concert with the reconstitution of fragments of this receptor, provided information on the molecular basis of these interactions. Development of three color fluorescence resonance energy transfer (FRET) allowed the imaging of alpha(1b)-adrenoceptor oligomers in single living cells. Mutation of hydrophobic residues in transmembrane domains I and IV of the receptor resulted in marked reduction in three color FRET suggesting an alteration in oligomeric organization and potential similarities with rhodopsin. The mutated alpha(1b)-adrenoceptor was unable to reach the cell surface, did not become terminally N-glycosylated and was unable to signal.

Publication Types:
Review

PMID: 17005232 [PubMed - indexed for MEDLINE]

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5: Curr Opin Struct Biol. 2006 Apr;16(2):252-9. Epub 2006 Mar 29.


Structure of the rhodopsin dimer: a working model for G-protein-coupled receptors.

Fotiadis D, Jastrzebska B, Philippsen A, Müller DJ, Palczewski K, Engel A.

ME Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.

G-protein-coupled receptors (GPCRs) participate in virtually all physiological processes. They constitute the largest and most structurally conserved family of signaling molecules. Several class C GPCRs have been shown to exist as dimers in their active form and growing evidence indicates that many, if not all, class A receptors also form dimers and/or higher-order oligomers. High-resolution crystal structures are available only for the detergent-solubilized light receptor rhodopsin (Rho), the archetypal class A GPCR. In addition, Rho is the only GPCR for which the presumed higher-order oligomeric state has been demonstrated, by imaging native disk membranes using atomic force microscopy (AFM). Based on these data and the X-ray structure, an atomic model of Rho dimers has been proposed, a model that is currently scrutinized in various ways. AFM has also been used to measure the forces required to unfold single Rho molecules, thereby revealing which residues are responsible for Rho's stability. Recent functional analyses of fractions from solubilized disk membranes revealed that higher-order Rho oligomers are the most active species. These and other results have enhanced our understanding of GPCR structure and function.

Publication Types:
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

PMID: 16567090 [PubMed - indexed for MEDLINE]

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6: Curr Opin Struct Biol. 2005 Aug;15(4):408-15.


Structure of rhodopsin and the metarhodopsin I photointermediate.

Schertler GF.

MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. gfx@mrc-lmb.cam.ac.uk

The structure of the visual pigment rhodopsin in the dark state was first investigated by electron microscopy (EM). More recently, rhodopsin has been crystallised in two different space groups--a tetragonal P4(1) crystal form and a trigonal P3(1) packing arrangement. The structures of the pigment, determined by X-ray crystallography from these two crystal forms, show many similarities, but also significant differences. These differences are most extensive in the G-protein-binding region of the cytoplasmic surface, where the location of the loop between helices 5 and 6 is highly variable. A combination of EM and spin labelling suggests that this loop adopts the native conformation in the P3(1) crystal form. The X-ray structures also show the location of structural water molecules that are important for colour tuning, stabilisation of the ground state and receptor activation, and act as a template for modelling other G-protein-coupled receptors. A major current focus of structural work on rhodopsin is investigation of the activated state of the receptor. After careful spectroscopic characterisation of light activation in two-dimensional crystals, a map of the metarhodopsin I intermediate was obtained by EM from two-dimensional crystals. In addition, NMR studies are providing information about the structure of activated states of rhodopsin. In the future, structural information will show how rhodopsin becomes activated and how it couples to downstream signalling pathways.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 16043340 [PubMed - indexed for MEDLINE]

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7: Med Clin (Barc). 2003 Jun 28;121(4):153-7.


[Rhodopsin structure: some light into the shadows of retinal degenerations]

[Article in Spanish]

Manyosa J, Andrés A, Buzón V, Garriga P.

Unitat de Biofísica. Departament de Bioquímica i de Biologia Molecular. Universitat Autònoma de Barcelona. Barcelona. Spain. joan.manyosa@uab.es

Retinitis pigmentosa is a group of retinal degenerative diseases, within the broad family of hereditary retinopathies, for which there is no cure at present. Mutations in different genes coding for proteins related to the metabolism of photoreceptor cells, and to the visual phototransduction cascade, are the cause of this disease. Rhodopsin, the photoreceptor protein responsible for light absorption--and key in the first stages of vision--is one of the most studied molecules of the retina. Mutations in the opsin gene account for about 25% of all cases of autosomal dominant retinitis pigmentosa. Recent crystallization of this receptor in its inactive dark state has revealed new structural details yielding further insights into the intra and intermolecular mechanismsin which the protein is involved as a result of its activation.Furthermore, the in vitro study of recombinant rhodopsins carrying mutations previously found in retinitis pigmentosa patients (by means of spectroscopic and functional techniques) has shed new light on the structural requirements for its correct function, as well as the molecular defects underlying the mechanism of photoreceptor cell death. In this study, the main findings of the recent investigations carried out in this field are presented. The relevant information obtained at the molecular level is bound to facilitate our understandingof the molecular processes that will allow suitable therapiesfor different retinal degenerative diseases, particularly retinitis pigmentosa, to be proposed.

Publication Types:
English Abstract
Research Support, Non-U.S. Gov't
Review

PMID: 12867022 [PubMed - indexed for MEDLINE]

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8: Curr Opin Drug Discov Devel. 2001 Sep;4(5):561-74.


G protein-coupled receptor drug discovery: implications from the crystal structure of rhodopsin.

Ballesteros J, Palczewski K.

Novasite Pharmaceuticals Inc., 3520 Dunhill Street, San Diego, CA 92121, USA. jballesteros@novasite.com

G protein-coupled receptors (GPCRs) are a functionally diverse group of membrane proteins that play a critical role in signal transduction. Because of the lack of a high-resolution structure, the heptahelical transmembrane bundle within the N-terminal extracellular and C-terminal intracellular region of these receptors has initially been modeled based on the high-resolution structure of bacterial retinal-binding protein, bacteriorhodopsin. However, the low-resolution structure of rhodopsin, a prototypical GPCR, revealed that there is a minor relationship between GPCRs and bacteriorhodopsins. The high-resolution crystal structure of the rhodopsin ground state and further refinements of the model provide the first structural information about the entire organization of the polypeptide chain and post-translational moieties. These studies provide a structural template for Family 1 GPCRs that has the potential to significantly improve structure-based approaches to GPCR drug discovery.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 12825452 [PubMed - indexed for MEDLINE]

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9: Adv Protein Chem. 2003;63:243-90.


Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking.

Hubbell WL, Altenbach C, Hubbell CM, Khorana HG.

Jules Stein Eye Institute, Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA.

Publication Types:
Review

PMID: 12629973 [PubMed - indexed for MEDLINE]

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10: Biochim Biophys Acta. 2002 Oct 11;1565(2):168-82.


Crystal structure of rhodopsin: a template for cone visual pigments and other G protein-coupled receptors.

Stenkamp RE, Filipek S, Driessen CA, Teller DC, Palczewski K.

Department of Biological Structure, University of Washington, Seattle, WA 98195, USA.

The crystal structure of rhodopsin has provided the first three-dimensional molecular model for a G-protein-coupled receptor (GPCR). Alignment of the molecular model from the crystallographic structure with the helical axes seen in cryo-electron microscopic (cryo-EM) studies provides an opportunity to investigate the properties of the molecule as a function of orientation and location within the membrane. In addition, the structure provides a starting point for modeling and rational experimental approaches of the cone pigments, the GPCRs in cone cells responsible for color vision. Homology models of the cone pigments provide a means of understanding the roles of amino acid sequence differences that shift the absorption maximum of the retinal chromophore in the environments of different opsins.

Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 12409193 [PubMed - indexed for MEDLINE]

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11: Receptors Channels. 2002;8(1):33-50.


Rhodopsin and retinitis pigmentosa: shedding light on structure and function.

Stojanovic A, Hwa J.

Department of Pharmacology and Toxicology, Dartmouth Medical School, Dartmouth College, 7650 Remsen, Hanover, NH 03755, USA.

Rhodopsin is the dim-light activated photoreceptor located in the rod cells of the eye. It belongs to the large superfamily of G-protein-coupled receptors (GPCRs). Many consider it the proto-typical GPCR as numerous studies since its cloning in 1983 (Nathans and Hogness 1983) have established many fundamental principles of seven transmembrane-spanning GPCRs. Abundant expression in the rod's outer segment, constituting about 90% of the total membrane protein in the discs, and the development of techniques to purify large quantities of functional protein has facilitated this process. Another distinct feature is rhodopsin's ligand, 11-cis-retinal, which is covalently bound via a Schiff base to transmembrane seven (TM VII), allowing extensive spectroscopic studies. Exciting recent developments include the discovery of naturally occurring mutations that lead to retinal degeneration, the determination of transmembrane movements using electron paramagnetic resonance (EPR) and biochemical techniques, and the discovery of its 3D X-ray crystal structure, the first among GPCRs. The impact of these major advances will be discussed in this review.

Publication Types:
Review

PMID: 12402507 [PubMed - indexed for MEDLINE]

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12: Chembiochem. 2002 Oct 4;3(10):963-7.


Crystal structure of rhodopsin: a G-protein-coupled receptor.

Stenkamp RE, Teller DC, Palczewski K.

Department of Biological Structure, University of Washington Seattle, WA 98195-7420, USA. stenkamp@u.washington.edu

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 12362360 [PubMed - indexed for MEDLINE]

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13: Curr Opin Struct Biol. 2002 Aug;12(4):540-6.


Sensory rhodopsin II: functional insights from structure.

Spudich JL, Luecke H.

Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77030, USA. John.L.Spudich@uth.tmc.edu

Atomic resolution structures of a sensory rhodopsin phototaxis receptor in haloarchaea (the first sensory member of the widespread microbial rhodopsin family) have yielded insights into the interaction face with its membrane-embedded transducer and into the mechanism of spectral tuning. Spectral differences between sensory rhodopsin and the light-driven proton pump bacteriorhodopsin depend largely upon the repositioning of a conserved arginine residue in the chromophore-binding pocket. Information derived from the structures, combined with biophysical and biochemical analysis, has established a model for receptor activation and signal relay, in which light-induced helix tilting in the receptor is transmitted to the transducer by lateral transmembrane helix-helix interactions.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 12163079 [PubMed - indexed for MEDLINE]

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14: Tanpakushitsu Kakusan Koso. 2002 Jun;47(8 Suppl):1123-30.


[Structure-function relationship in G protein-coupled receptors deduced from crystal structure of rhodopsin]

[Article in Japanese]

Okada T, Terakita A, Shichida Y.

t-okada@aist.go.jp

Publication Types:
Review

PMID: 12099033 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

15: Curr Opin Cell Biol. 2002 Apr;14(2):189-95.


Structure of rhodopsin and the superfamily of seven-helical receptors: the same and not the same.

Sakmar TP.

Howard Hughes Medical Institute, Laboratory of Molecular Biology and Biochemistry, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. sakmar@mail.rockefeller.edu

The crystal structure of rhodopsin provides significant insights concerning structure/activity relationships in visual pigments and related G-protein-coupled receptors. The specific arrangement of seven-transmembrane helices is stabilized by a series of intermolecular interactions that appear to be conserved among Family A receptors. However, the potential for structural and functional diversity among members of the superfamily of seven-helical receptors presents a significant future challenge.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 11891118 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

16: Trends Pharmacol Sci. 2001 Nov;22(11):587-93.


Receptor activation: what does the rhodopsin structure tell us?

Meng EC, Bourne HR.

Dept of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143-0450, USA.

G-protein-coupled receptors (GPCRs) are a large family of seven-transmembrane-helix proteins that mediate responses to hormones, neurotransmitters and, in the case of rhodopsin, photons. The recent determination of the structure of rhodopsin at atomic resolution opens avenues to a deeper understanding of GPCR activation and transmembrane signaling. Data from previous crosslinking, spin labeling and scanning accessibility experiments on rhodopsin have been mapped onto the high-resolution structure. These data correlate well and are consistent with the structure, and suggest that activation by light opens a cleft at the cytoplasmic end of the seven-helix bundle of rhodopsin. Furthermore, lessons learned from rhodopsin might also apply to other members of this essential family of receptors. (For an animation of the crystal structure of rhodopsin see http://archive.bmn.com/supp/tips/tips2211a.html)

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 11698103 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

17: Curr Opin Struct Biol. 2001 Aug;11(4):420-6.


Crystal structure of rhodopsin: implications for vision and beyond.

Okada T, Palczewski K.

Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan. okada@photo2.biophys.kyoto-u.ac.jp

A heptahelical transmembrane bundle is a common structural feature of G-protein-coupled receptors (GPCRs) and bacterial retinal-binding proteins, two functionally distinct groups of membrane proteins. Rhodopsin, a photoreceptor protein involved in photopic (rod) vision, is a prototypical GPCR that contains 11-cis-retinal as its intrinsic chromophore ligand. Therefore, uniquely, rhodopsin is a GPCR and also a retinal-binding protein, but is not found in bacteria. Rhodopsin functions as a typical GPCR in processes that are triggered by light and photoisomerization of its ligand. Bacteriorhodopsin is a light-driven proton pump with an all-trans-retinal chromophore that photoisomerizes to 13-cis-retinal. The recent crystal structure determination of bovine rhodopsin revealed a structure that is not similar to previously established bacteriorhodopsin structures. Both groups of proteins have a heptahelical transmembrane bundle structure, but the helices are arranged differently. The activation of rhodopsin involves rapid cis-trans photoisomerization of the chromophore, followed by slower and incompletely defined structural rearrangements. For rhodopsin and related receptors, a common mechanism is predicted for the formation of an active state intermediate that is capable of interacting with G proteins.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 11495733 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

18: Biochemistry. 2001 Jul 3;40(26):7761-72.


Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs).

Teller DC, Okada T, Behnke CA, Palczewski K, Stenkamp RE.

Department of Ophthalmology, and Biological Structure and Biomolecular Structure Center, University of Washington, Seattle, Washington 98195, USA. teller@u.washington.edu

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 11425302 [PubMed - indexed for MEDLINE]

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19: Mol Pharmacol. 2001 Jul;60(1):1-19.


Erratum in:
Mol Pharmacol 2002 Jan;61(1):247.

Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors.

Ballesteros JA, Shi L, Javitch JA.

Novasite Pharmaceuticals, Inc., San Diego, California, USA. jaj2@columbia.edu

The availability of a high-resolution structure of rhodopsin now allows us to reconsider research attempts to understand structure-function relationships in other G protein-coupled receptors (GPCRs). A comparison of the rhodopsin structure with the results of previous sequence analysis and molecular modeling that incorporated experimental results demonstrates a high degree of success for these methods in predicting the helix ends and protein-protein interface of GPCRs. Moreover, the amino acid residues inferred to form the surface of the binding-site crevice based on our application of the substituted-cysteine accessibility method in the dopamine D(2) receptor are in remarkable agreement with the rhodopsin structure, with the notable exception of some residues in the fourth transmembrane segment. Based on our analysis of the data reviewed, we propose that the overall structures of rhodopsin and of amine receptors are very similar, although we also identified localized regions where the structure of these receptors may diverge. We further propose that several of the highly unusual structural features of rhodopsin are also present in amine GPCRs, despite the absence of amino acids that might have thought to have been critical to the adoption of these features. Thus, different amino acids or alternate microdomains can support similar deviations from regular alpha-helical structure, thereby resulting in similar tertiary structure. Such structural mimicry is a mechanism by which a common ancestor could diverge sufficiently to develop the selectivity necessary to interact with diverse signals, while still maintaining a similar overall fold. Through this process, the core function of signaling activation through a conformational change in the transmembrane segments that alters the conformation of the cytoplasmic surface and subsequent interaction with G proteins is presumably shared by the entire Class A family of receptors, despite their selectivity for a diverse group of ligands.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 11408595 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

20: Tanpakushitsu Kakusan Koso. 2001 May;46(6):687-97.


[Atomic structure of bovine rhodopsin, a seven transmembrane receptor: toward the elucidation of GPCR's molecular mechanism]

[Article in Japanese]

Miyano M, Kumasaka T, Hori T, Yamamoto M.

miyano@spring8.or.jp

Publication Types:
Review

PMID: 11360492 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

21: Invest Ophthalmol Vis Sci. 2001 Jan;42(1):3-9.


Rhodopsin structure, function, and topography the Friedenwald lecture.

Hargrave PA.

Department of Ophthalmology, School of Medicine, University of Florida, Gainesville, Florida 32610, USA. hargrave@ufl.edu

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 11133841 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

22: Novartis Found Symp. 1999;224:54-66; discussion 66-9,.


Structure of rhodopsin.

Schertler GF.

MRC Laboratory of Molecular Biology, Cambridge, UK.

Two-dimensional crystals of rhodopsin were studied to determine the arrangement of the transmembrane alpha helices. A combination of electron cryomicroscopy, image processing and electron crystallography was used to extract amplitudes and phases from images, and a three-dimensional map to a resolution of 7.5 A was calculated. Density peaks for all seven transmembrane helices were observed and the helix axes for all seven helices could be estimated. Near the intracellular side, which interacts with the G protein transducin, we observed three layers of helices arranged differently from bacteriorhodopsin. The arrangement opens up towards the extracellular side forming a cavity that serves as the binding pocket for the retinal. This cavity is closed towards the intracellular side by the long and highly tilted helix 3, and must be closed towards the extracellular side by the loop linking helices 4 and 5 which is linked by a disulfide bridge to the extracellular end of helix 3.

Publication Types:
Review

PMID: 10614046 [PubMed - indexed for MEDLINE]

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23: Eye. 1998;12 ( Pt 3b):504-10.


Structure of rhodopsin.

Schertler GF.

MRC Laboratory of Molecular Biology, Cambridge, UK. gfx@mrc-lmb.cam.ac.uk

Two-dimensional crystals of rhodopsin were studied to determine the arrangement of the transmembrane alpha helices. A combination of electron cryo-microscopy, image processing and electron crystallography was used to extract amplitudes and phases from images, and a three-dimensional map to a resolution of 7.5 A was calculated. Density peaks for all seven transmembrane helices were observed and the helix axes for all seven helices could be estimated. Near the intracellular side, which interacts with the G protein transducin, we observed three layers of helices arranged differently from bacteriorhodopsin. The arrangement opens up towards the extracellular side forming a cavity that serves as the binding pocket for the retinal. This cavity is closed towards the intracellular side by the long and highly tilted helix 3, and must be closed towards the extracellular side by the loop linking helices 4 and 5 that is linked by a disulphide bridge to the extracellular end of helix 3.

Publication Types:
Review

PMID: 9775210 [PubMed - indexed for MEDLINE]

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24: Biochem Soc Trans. 1998 Aug;26(3):520-31.


Structure of the G-protein-coupled receptor, rhodopsin: a domain approach.

Yeagle PL, Albert AD.

Department of Molecular and Cell Biology U-125, University of Connecticut, Storrs 06269, USA.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 9765908 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

25: Biochemistry. 1992 Jun 2;31(21):4923-31.


Rhodopsin: structure, function, and genetics.

Nathans J.

Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 1599916 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

26: J Biol Chem. 1992 Jan 5;267(1):1-4.


Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function.

Khorana HG.

Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 1730574 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

27: Kidney Int Suppl. 1987 Dec;23:S2-13.


Structure and function of the beta 2-adrenergic receptor--homology with rhodopsin.

Dohlman HG, Caron MG, Lefkowitz RJ.

Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, North Carolina.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2831423 [PubMed - indexed for MEDLINE]

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28: Photochem Photobiol. 1987 Jun;45(6):909-14.


Structure of rhodopsin and bacteriorhodopsin.

Ovchinnikov YA.

Publication Types:
Review

PMID: 3306728 [PubMed - indexed for MEDLINE]

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29: FEBS Lett. 1982 Nov 8;148(2):179-91.


Rhodopsin and bacteriorhodopsin: structure-function relationships.

Ovchinnikov YuA .

Publication Types:
Review

PMID: 6759163 [PubMed - indexed for MEDLINE]

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30: Usp Sovrem Biol. 1971 Sep-Oct;72(2):200-18.


[Rhodopsin: structure and transformations]

[Article in Russian]

Etingof RN, Ostapenko IA.

Publication Types:
Review

PMID: 4946796 [PubMed - indexed for MEDLINE]
 

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