FEBS Letters
Volume 582, Issue 6 , Pages 991-996, 19 March 2008

Dark and photoactivated rhodopsin share common binding modes to transducin

Edited by Robert B. Russell

Dulbecco Telethon Institute and Department of Chemistry, via Campi 183, 41100 Modena, Italy

Received 23 November 2007; received in revised form 7 February 2008; accepted 19 February 2008. published online 26 February 2008.

Abstract 

The structure of the photoactivated deprotonated rhodopsin intermediate was compared with two different structures of dark rhodopsin. Structure comparisons relied on the computation of molecular indices and on docking simulations with heterotrimeric transducin (Gt).

The results of this study provide the first evidence that dark and photoactivated rhodopsins share a common recognition mode to Gt, characterized by the docking of the Gtα C-tail in the proximity to the E/DRY motif of rhodopsin.

Keywords: Molecular recognition, Protein–protein docking, Computational modeling, GPCRs, G protein

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PII: S0014-5793(08)00159-2

doi:10.1016/j.febslet.2008.02.041

FEBS Letters
Volume 582, Issue 6 , Pages 991-996, 19 March 2008

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