Retinal Flip in Rhodopsin Activation?

Jun Feng, Michael F Brown, Blake Mertz

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)2767-2770
Number of pages4
JournalBiophysical Journal
Volume108
Issue number12
DOIs
StatePublished - Jun 18 2015

Fingerprint

Rhodopsin
Molecular Dynamics Simulation
Polyenes
Structural Models
G-Protein-Coupled Receptors
X-Rays
Ligands

ASJC Scopus subject areas

  • Biophysics

Cite this

Retinal Flip in Rhodopsin Activation? / Feng, Jun; Brown, Michael F; Mertz, Blake.

In: Biophysical Journal, Vol. 108, No. 12, 18.06.2015, p. 2767-2770.

Research output: Contribution to journalArticle

Feng, Jun ; Brown, Michael F ; Mertz, Blake. / Retinal Flip in Rhodopsin Activation?. In: Biophysical Journal. 2015 ; Vol. 108, No. 12. pp. 2767-2770.
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