The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue.
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.
Hirshberg
M
M
Division of Protein Structure, National Institute for Medical Research, Mill Hill, London, UK.
Stockley
R W
RW
Dodson
G
G
Webb
M R
MR
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D006165:Guanylyl Imidodiphosphate / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D020744:rac GTP-Binding Proteins; D018631:ras Proteins / Q000737:chemistry*
D011994:Recombinant Proteins; D006165:Guanylyl Imidodiphosphate; D019204:GTP-Binding Proteins; D020744:rac GTP-Binding Proteins; D018631:ras Proteins