The 2.2 Å crystal structure of transducin-α complexed with GTPγS
- 1 December 1993
- journal article
- Published by Springer Nature in Nature
- Vol. 366 (6456) , 654-663
- https://doi.org/10.1038/366654a0
Abstract
The 2.2 A crystal structure of activated rod transducin, Gt alpha.GTP gamma S, shows the bound GTP gamma S molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins. The structure, when combined with biochemical and genetic studies, suggests: how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanism for GTPase activity not evident from previous data.Keywords
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