Muscarinic Acetylcholine Receptor Structure
Published by Anonymous on 2007/9/30 (4467 reads)
1: Prog Brain Res. 1993;98:121-7.
Muscarinic acetylcholine receptor subtypes: localization and structure/function.
Brann MR, Ellis J, Jørgensen H, Hill-Eubanks D, Jones SV.
Department of Psychiatry, University of Vermont, Burlington 05405.
Based on the sequence of the five cloned muscarinic receptor subtypes (m1-m5), subtype selective antibody and cDNA probes have been prepared. Use of these probes has demonstrated that each of the five subtypes has a markedly distinct distribution within the brain and among peripheral tissues. The distributions of these subtypes and their potential physiological roles are discussed. By use of molecular genetic manipulation of cloned muscarinic receptor cDNAs, the regions of muscarinic receptors that specify G-protein coupling and ligand binding have been defined in several recent studies. Overall, these studies have shown that amino acids within the third cytoplasmic loop of the receptors define their selectivities for different G-proteins and that multiple discontinuous epitopes contribute to their selectivities for different ligands. The residues that contribute to ligand binding and G-protein coupling are described, as well as the implied structures of these functional domains.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 8248499 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Trends Pharmacol Sci. 1989 Dec;Suppl:22-5.
Localization and structure of the muscarinic receptor ligand binding site.
Hulme EC, Curtis CA, Wheatley M, Aitken A, Harris AC.
A conserved aspartic acid residue in transmembrane helix 3 of the muscarinic acetylcholine receptors is important in binding the headgroup of muscarinic ligands. This acidic amino acid probably points into a relatively hydrophilic cavity whose walls are formed by the amphipathic transmembrane helices of the receptor. Amino acid side chains within this cavity contribute to ligand binding.
Publication Types:
Review
PMID: 2694518 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Trends Pharmacol Sci. 1988 Feb;Suppl:19-24.
Peptide mapping studies on muscarinic receptors: receptor structure and location of the ligand binding site.
Wheatley M, Hulme EC, Birdsall NJ, Curtis CA, Eveleigh P, Pedder EK, Poyner D.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 3074531 [PubMed - indexed for MEDLINE]
Muscarinic acetylcholine receptor subtypes: localization and structure/function.
Brann MR, Ellis J, Jørgensen H, Hill-Eubanks D, Jones SV.
Department of Psychiatry, University of Vermont, Burlington 05405.
Based on the sequence of the five cloned muscarinic receptor subtypes (m1-m5), subtype selective antibody and cDNA probes have been prepared. Use of these probes has demonstrated that each of the five subtypes has a markedly distinct distribution within the brain and among peripheral tissues. The distributions of these subtypes and their potential physiological roles are discussed. By use of molecular genetic manipulation of cloned muscarinic receptor cDNAs, the regions of muscarinic receptors that specify G-protein coupling and ligand binding have been defined in several recent studies. Overall, these studies have shown that amino acids within the third cytoplasmic loop of the receptors define their selectivities for different G-proteins and that multiple discontinuous epitopes contribute to their selectivities for different ligands. The residues that contribute to ligand binding and G-protein coupling are described, as well as the implied structures of these functional domains.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 8248499 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Trends Pharmacol Sci. 1989 Dec;Suppl:22-5.
Localization and structure of the muscarinic receptor ligand binding site.
Hulme EC, Curtis CA, Wheatley M, Aitken A, Harris AC.
A conserved aspartic acid residue in transmembrane helix 3 of the muscarinic acetylcholine receptors is important in binding the headgroup of muscarinic ligands. This acidic amino acid probably points into a relatively hydrophilic cavity whose walls are formed by the amphipathic transmembrane helices of the receptor. Amino acid side chains within this cavity contribute to ligand binding.
Publication Types:
Review
PMID: 2694518 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Trends Pharmacol Sci. 1988 Feb;Suppl:19-24.
Peptide mapping studies on muscarinic receptors: receptor structure and location of the ligand binding site.
Wheatley M, Hulme EC, Birdsall NJ, Curtis CA, Eveleigh P, Pedder EK, Poyner D.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 3074531 [PubMed - indexed for MEDLINE]
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