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The 2.2 Å crystal structure of transducin- complexed with GTP S 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, Gt -GTP S, shows the bound GTP 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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