Characterizing and predicting the functional and conformational diversity of seven-transmembrane proteins.

ABSTRACT: The activation of seven-transmembrane receptors (7TMRs) allows cells to sense their environment and convert extracellular signals (like hormone binding) into intracellular signals (through G protein-coupled and/or β arrestin-coupled pathways). A single 7TMR is capable of transducing a wide spectrum of physiological responses inside a cell by coupling to these pathways. This intracellular pleiotropic action is enabled by multiple conformations exhibited by these receptors. Developments in membrane protein structure determination technologies have led to a rapid increase in crystal structures for many 7TMRs. Majority of these receptors have been crystallized in their inactive conformation and, for some, one of the many active conformations has also been crystallized. Given the topological co

SUBMITTER: Abrol R 

PROVIDER: S-EPMC3286597 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature