Dark and photoactivated rhodopsin share common binding modes to transducin.
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 Gt alpha C-tail in the proximity to the E/DRY motif of rhodopsin.
Fanelli
Francesca
F
Dulbecco Telethon Institute and Department of Chemistry, via Campi 183, 41100 Modena, Italy. fanelli@unimo.it <fanelli@unimo.it>
Dell'orco
Daniele
D
D003624:Darkness; D008027:Light; D011487:Protein Conformation / Q000528:radiation effects; D012243:Rhodopsin / Q000737:chemistry* / Q000528:radiation effects; D015293:Transducin / Q000737:chemistry* / Q000528:radiation effects
D012243:Rhodopsin; D015293:Transducin