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PMID: 21278756 Published · ppublish English Journal Article Research Support, N.I.H., Extramural

Retinal dynamics underlie its switch from inverse agonist to agonist during rhodopsin activation.

Nature structural & molecular biology ·Vol. 18 ·No. 3 ·2011-03-00 ·Pages 392-4

Struts AV, Salgado GF, Martínez-Mayorga K, Brown MF

Abstract

X-ray and magnetic resonance approaches, though central to studies of G protein-coupled receptor (GPCR)-mediated signaling, cannot address GPCR protein dynamics or plasticity. Here we show that solid-state (2)H NMR relaxation elucidates picosecond-to-nanosecond-timescale motions of the retinal ligand that influence larger-scale functional dynamics of rhodopsin in membranes. We propose a multiscale activation mechanism whereby retinal initiates collective helix fluctuations in the meta I-meta II equilibrium on the microsecond-to-millisecond timescale.

MeSH Terms
Animals Cattle Models, Molecular Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Conformation Retinaldehyde/chemistry,metabolism Rhodopsin/chemistry,metabolism
Chemicals
Rhodopsin Retinaldehyde
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Struts Andrey V
Department of Chemistry, University of Arizona, Tucson, AZ, USA.
Salgado Gilmar F J
Martínez-Mayorga Karina
Brown Michael F
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Article Info
Journal
Nature structural & molecular biology
Abbr.
Nat Struct Mol Biol
ISSN
1545-9985
Published
2011-03-00
Epub
2011-00-30
Pages
392-4
Language
English
Region
United States
NLM ID
101186374
PMCID
PMC5283944
Subset
IM
Grants
NEI NIH HHS · R01 EY012049 · United States
NEI NIH HHS · R01 EY018891 · United States
NEI NIH HHS · EY018891 · United States
NEI NIH HHS · EY012049 · United States
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