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 addition to the previously reported tilting and bending. These hitherto undefined motion components unify the results obtained from different experimental approaches, and demonstrate conformational similarity between the active opsin structure and the photoactivated structures in crystallo near the retinal anchor despite their marked differences.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Ren Z,Ren PX,Balusu R,Yang X

doi

10.1038/srep34129

subject

Has Abstract

pub_date

2016-09-23 00:00:00

pages

34129

issn

2045-2322

pii

srep34129

journal_volume

6

pub_type

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