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Biochemistry. 2005 Nov 15;44(45):14695-700.

Rhodopsin activation follows precoupling with transducin: inferences from computational analysis.

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Department of Chemistry, University of Modena and Reggio Emilia, and Dulbecco Telethon Institute, via Campi 183 41100 Modena, Italy.


The electrostatic and shape complementarities between the crystal structures of dark rhodopsin and heterotrimeric transducin (Gt) have been evaluated by exhaustively sampling the roto-translational space of one protein with respect to the other. Structural complementarity, reliability, and consistency with in vitro evidence all converge in the same rhodopsin-Gt complex, showing that the functionally important R135 of the E/DRY motif is almost accessible to the C-terminus of Gt(alpha) already in the dark state. The main inference from this study is that activation of rhodopsin and Gt may be concurrent processes, consisting of conformational changes in a supramolecular complex formed prior to the light-induced activation of the photoreceptor.

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