Coarse-grained modeling of allosteric regulation in protein receptors.

ABSTRACT: Allosteric regulation provides highly specific ligand recognition and signaling by transmembrane protein receptors. Unlike functions of protein molecular machines that rely on large-scale conformational transitions, signal transduction in receptors appears to be mediated by more subtle structural motions that are difficult to identify. We describe a theoretical model for allosteric regulation in receptors that addresses a fundamental riddle of signaling: What are the structural origins of the receptor agonism (specific signaling response to ligand binding)? The model suggests that different signaling pathways in bovine rhodopsin or human beta(2)-adrenergic receptor can be mediated by specific structural motions in the receptors. We discuss implications for understanding the receptor agonis

SUBMITTER: Balabin IA 

PROVIDER: S-EPMC2732817 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature