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The 2.2 Å crystal structure of transducin-α complexed with GTPγS

Naturevolume 366pages654663 (1993) | Download Citation

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Abstract

The 2.2 Å crystal structure of activated rod transducin, G-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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Author notes

  1. Paul B. Sigler: To whom correspondence should be addressed.

Affiliations

  1. Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, Boyer Center for Molecular Medicine, 295 Congress Avenue, Room 154, New Haven, Connecticut, 06510, USA

    • Joseph P. Noel
    •  & Paul B. Sigler
  2. Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, Illinois, 60680, USA

    • Heidi E. Hamm
  3. Istituto di Fisiologia Generale e Chimica Biologica, Universita' di Sassari, 07100, Sassari, Italy

    • Heidi E. Hamm

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https://doi.org/10.1038/366654a0

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