Localization and structure of the muscarinic receptor ligand binding site

E. C. Hulme; C. A.M. Curtis; M. Wheatly; A. Aitken; A. C. Harris

Localization and structure of the muscarinic receptor ligand binding site

E. C. Hulme
, C. A.M. Curtis
, M. Wheatly
, A. Aitken
, A. C. Harris

MRC National Institute for Medical Research

Research output: Contribution to journal › Article › peer-review

18 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	22-25
Number of pages	4
Journal	Trends in Pharmacological Sciences
Volume	10
Issue number	SUPPL.
Publication status	Published - 1 Dec 1989
Externally published	Yes

ASJC Scopus subject areas

Toxicology
Pharmacology

Cite this

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title = "Localization and structure of the muscarinic receptor ligand binding site",

abstract = "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.",

author = "Hulme, \{E. C.\} and Curtis, \{C. A.M.\} and M. Wheatly and A. Aitken and Harris, \{A. C.\}",

year = "1989",

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language = "English",

volume = "10",

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journal = "Trends in Pharmacological Sciences",

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TY - JOUR

T1 - Localization and structure of the muscarinic receptor ligand binding site

AU - Hulme, E. C.

AU - Curtis, C. A.M.

AU - Wheatly, M.

AU - Aitken, A.

AU - Harris, A. C.

PY - 1989/12/1

Y1 - 1989/12/1

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0024472063

M3 - Article

C2 - 2694518

AN - SCOPUS:0024472063

SN - 0165-6147

VL - 10

SP - 22

EP - 25

JO - Trends in Pharmacological Sciences

JF - Trends in Pharmacological Sciences

IS - SUPPL.

ER -

Localization and structure of the muscarinic receptor ligand binding site

Abstract

ASJC Scopus subject areas

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