Transmembrane Helices Tilt, Bend, Slide, Torque, and Unwind between Functional States of Rhodopsin.

ABSTRACT: The seven-helical bundle of rhodopsin and other G-protein coupled receptors undergoes structural rearrangements as the transmembrane receptor protein is activated. These structural changes are known to involve tilting and bending of various transmembrane helices. However, the cause and effect relationship among structural events leading to a cytoplasmic crevasse for G-protein binding is less well defined. Here we present a mathematical model of the protein helix and a simple procedure to determine multiple parameters that offer precise depiction of a helical conformation. A comprehensive survey of bovine rhodopsin structures shows that the helical rearrangements during the activation of rhodopsin involve a variety of angular and linear motions such as torsion, unwinding, and sliding in add

SUBMITTER: Ren Z 

PROVIDER: S-EPMC5034245 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature