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, C-tail in the proximity to the E/DRY motif of rhodopsin. (C) 2008 Federation of European Biochemical Societies.
Dark and photoactivated rhodopsin share common binding modes to transducin.
DELL'ORCO, Daniele
2008-01-01
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, C-tail in the proximity to the E/DRY motif of rhodopsin. (C) 2008 Federation of European Biochemical Societies.
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