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.

Dark and photoactivated rhodopsin share common binding modes to transducin / Fanelli, Francesca; D., Dell'Orco. - In: FEBS LETTERS. - ISSN 0014-5793. - ELETTRONICO. - 582:(2008), pp. 991-996. [10.1016/j.febslet.2008.02.041]

Dark and photoactivated rhodopsin share common binding modes to transducin

FANELLI, Francesca;
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 Gt alpha C-tail in the proximity to the E/DRY motif of rhodopsin.
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Dark and photoactivated rhodopsin share common binding modes to transducin / Fanelli, Francesca; D., Dell'Orco. - In: FEBS LETTERS. - ISSN 0014-5793. - ELETTRONICO. - 582:(2008), pp. 991-996. [10.1016/j.febslet.2008.02.041]
Fanelli, Francesca; D., Dell'Orco
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/610789
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