Abstract
The 2.2 Å crystal structure of activated rod transducin, Gtα-GTPγS, shows the bound GTPγS 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.
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Noel, J., Hamm, H. & Sigler, P. The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366, 654–663 (1993). https://doi.org/10.1038/366654a0
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DOI: https://doi.org/10.1038/366654a0
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