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Title
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The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S.
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Authors
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J.P.Noel,
H.E.Hamm,
P.B.Sigler.
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Ref.
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Nature, 1993,
366,
654-663.
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PubMed id
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Abstract
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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.
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