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The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue

Nature Structural Biology volume 4, pages 147–152 (1997)Cite this article

Abstract

The crystal structure of human racl, a member of the rho family of small G-proteins, complexed with the non-hydrolysable GTP analogue, guanosine-5′-(βγ-imino)triphosphate (GMPPNP), has been determined by X-ray analysis at a resolution of 1.38 Å. Comparison with the structure of H-ras indicates that racl has an extra α-helical domain that is characteristic of the rho G proteins, and may be involved in the signalling pathway of this family.

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Authors and Affiliations

  1. Division of Protein Structure, The National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, UK

    Miriam Hirshberg & Guy Dodson

  2. Division of Physical Biochemistry, The National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, UK

    Richard W. Stockley & Martin R. Webb

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  1. Miriam Hirshberg
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  2. Richard W. Stockley
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  3. Guy Dodson
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  4. Martin R. Webb
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Hirshberg, M., Stockley, R., Dodson, G. et al. The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nat Struct Mol Biol 4, 147–152 (1997). https://doi.org/10.1038/nsb0297-147

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