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.

Rhodopsin activation follows precoupling with transducin: Inferences from computational analysis / Fanelli, Francesca; D., Dell'Orco. - In: BIOCHEMISTRY. - ISSN 0006-2960. - ELETTRONICO. - 44(2005), pp. 14695-14700.

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