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Biophys J. 2015 Jun 16;108(12):2767-70. doi: 10.1016/j.bpj.2015.04.040.

Retinal Flip in Rhodopsin Activation?

Author information

1
The C. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia.
2
Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona; Department of Physics, University of Arizona, Tucson, Arizona.
3
The C. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia. Electronic address: blake.mertz@mail.wvu.edu.

Abstract

Rhodopsin is a well-characterized structural model of a G protein-coupled receptor. Photoisomerization of the covalently bound retinal triggers activation. Surprisingly, the x-ray crystal structure of the active Meta-II state has a 180° rotation about the long-axis of the retinal polyene chain. Unbiased microsecond-timescale all-atom molecular dynamics simulations show that the retinal cofactor can flip back to the orientation observed in the inactive state of rhodopsin under conditions favoring the Meta-I state. Our results provide, to our knowledge, the first evidence from molecular dynamics simulations showing how rotation of the retinal ligand within its binding pocket can occur in the activation mechanism of rhodopsin.

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PMID:
26083914
PMCID:
PMC4472225
DOI:
10.1016/j.bpj.2015.04.040
[Indexed for MEDLINE]
Free PMC Article

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