Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/23515
Title: Structural interpretation of P2X receptor mutagenesis studies on drug action.
Authors: Evans, RJ
First Published: Nov-2010
Citation: BR J PHARMACOL, 2010, 161 (5), pp. 961-971
Abstract: P2X receptors for ATP are ligand gated cation channels that form from the trimeric assembly of subunits with two transmembrane segments, a large extracellular ligand binding loop, and intracellular amino and carboxy termini. The receptors are expressed throughout the body, involved in functions ranging from blood clotting to inflammation, and may provide important targets for novel therapeutics. Mutagenesis based studies have been used to develop an understanding of the molecular basis of their pharmacology with the aim of developing models of the ligand binding site. A crystal structure for the zebra fish P2X4 receptor in the closed agonist unbound state has been published recently, which provides a major advance in our understanding of the receptors. This review gives an overview of mutagenesis studies that have led to the development of a model of the ATP binding site, as well as identifying residues contributing to allosteric regulation and antagonism. These studies are discussed with reference to the crystal to provide a structural interpretation of the molecular basis of drug action.
DOI Link: 10.1111/j.1476-5381.2010.00728.x
eISSN: 1476-5381
Links: http://hdl.handle.net/2381/23515
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Cell Physiology and Pharmacology

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