期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 396, 期 3, 页码 510-527出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.12.003
关键词
rhodopsin; G-protein-coupled receptors; NMR; molecular dynamics; retinal
资金
- National Institutes of Health-National Science Foundation [S10 RR13889, DBI-9977553]
- National Institutes of Health [GM-41412]
- Kimmelman Center for Biomolecular Structure and Assembly
- United States-Israel Binational Science Foundation
Structural restraints provided by solid-state NMR measurements of the metarhodopsin 11 intermediate are combined with molecular dynamics simulations to help visualize structural changes in the light activation of rhodopsin. Since the timescale for the formation of the metarhodopsin H intermediate (>1 ms) is beyond that readily accessible by molecular dynamics, we use NMR distance restraints derived from C-13 dipolar recoupling measurements to guide the simulations. The simulations yield a working model for how photoisomerization of the 11-cis retinylidene chromophore bound within the interior of rhodopsin is coupled to transmembrane helix motion and receptor activation. The mechanism of activation that emerges is that multiple switches on the extracellular (or intradiscal) side of rhodopsin trigger structural changes that converge to disrupt the ionic lock between helices H3 and H6 on the intracellular side of the receptor. (C) 2009 Elsevier Ltd. All rights reserved.
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