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Structural determinants for activation of the α-subunit of a heterotrimeric G protein

Nature volume 369, pages 621–628 (1994)Cite this article

Abstract

The 1.8 Å crystal structure of transducin α-GDP, when compared to that of the activated complex with GTP-γS, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein α-subunit. Structural changes initiated by direct contacts with the terminal phosphate of GTP propagate to regions that have been implicated in effector activation. The changes are distinct from those observed in other members of the GTPase superfamily.

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Author notes

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

Authors and Affiliations

  1. The 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

    David G. Lambright, Joseph P. Noel & Paul B. Sigler

  2. Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, Illinois, 60612, USA

    Heidi E. Hamm

  3. Structural Biology Laboratory, The Salk Institute for Biological Studies, PO Box 85800, San Diego, California, 92186-5800, USA

    Joseph P. Noel

Authors
  1. David G. Lambright
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  2. Joseph P. Noel
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  3. Heidi E. Hamm
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  4. Paul B. Sigler
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Lambright, D., Noel, J., Hamm, H. et al. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 369, 621–628 (1994). https://doi.org/10.1038/369621a0

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