期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 32, 期 -, 页码 873-877出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST0320873
关键词
allosteric interaction; drug discovery; G-protein-coupled receptor; kinetics; ternary complex model
Allosteric modulators of G-protein-coupled receptors interact with binding sites that are topographically distinct from the orthosteric site recognized by the receptor's endogenous agonist. Allosteric ligands offer a number of advantages over orthosteric drugs, including the potential for greater receptor subtype selectivity and a more 'physiological' regulation of receptor activity. However, the manifestations of allosterism at G-protein-coupled receptors are quite varied, and significant challenges remain for the optimization of screening methods to ensure the routine detection and validation of allosteric ligands.
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