The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S.

Noel JP, Hamm HE, Sigler PB
Nature. 1993 366 (6456): 654-63

PMID: 8259210 · DOI:10.1038/366654a0

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.

MeSH Terms (18)

Amino Acid Sequence Animals Catalysis Cattle Computer Graphics Crystallography, X-Ray Guanosine 5'-O-(3-Thiotriphosphate) Guanosine Diphosphate Guanosine Triphosphate Hydrolysis Models, Molecular Molecular Sequence Data Phosphoric Diester Hydrolases Protein Binding Protein Conformation Retinal Rod Photoreceptor Cells Rhodopsin Transducin

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