Putative active states of a prototypic g-protein-coupled receptor from biased molecular dynamics.

ABSTRACT: A major current focus of structural work on G-protein-coupled receptors (GPCRs) pertains to the investigation of their active states. However, for virtually all GPCRs, active agonist-bound intermediate states have been difficult to characterize experimentally owing to their higher conformational flexibility, and thus intrinsic instability, as compared to inactive inverse agonist-bound states. In this work, we explored possible activation pathways of the prototypic GPCR bovine rhodopsin by means of biased molecular dynamics simulations. Specifically, we used an explicit atomistic representation of the receptor and its environment, and sampled the conformational transition from the crystal structure of a photoactivated deprotonated state of rhodopsin to the low pH crystal structure of opsin

SUBMITTER: Provasi D 

PROVIDER: S-EPMC2872269 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature