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Article
Nature 366, 654 - 663 (16 December 1993); doi:10.1038/366654a0

The 2.2 Å crystal structure of transducin-alpha complexed with GTPbig gammaS

Joseph P. Noel*, Heidi E. Hamm†‡ & Paul B. Sigler

* Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, 295 Congress Avenue, Boyer Center for Molecular Medicine, Room 154, New Haven, Connecticut 06510, USA
Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, Illinois 60680, USA
Istituto di Fisiologia Generale e Chimica Biologica, Universita' di Sassari, 07100 Sassari, Italy
§ To whom correspondence should be addressed.

The 2.2 Å crystal structure of activated rod transducin, Gtalpha-GTPbold gammaS, shows the bound GTPbold gammaS 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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