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

Nat Struct Biol. 1997 Feb;4(2):147-52. doi: 10.1038/nsb0297-147.

Abstract

The crystal structure of human rac1, a member of the rho family of small G-proteins, complexed with the non-hydrolysable GTP analogue, guanosine-5'-(beta gamma-imino)triphosphate (GMPPNP), has been determined by X-ray analysis at a resolution of 1.38 A. Comparison with the structure of H-ras indicates that rac1 has an extra alpha-helical domain that is characteristic of the rho G proteins, and may be involved in the signalling pathway of this family.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • GTP-Binding Proteins / chemistry*
  • GTP-Binding Proteins / metabolism*
  • Guanylyl Imidodiphosphate / chemistry
  • Guanylyl Imidodiphosphate / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • rac GTP-Binding Proteins
  • ras Proteins / chemistry*

Substances

  • Recombinant Proteins
  • Guanylyl Imidodiphosphate
  • GTP-Binding Proteins
  • rac GTP-Binding Proteins
  • ras Proteins