Article
X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis.
Proceedings of the National Academy of Sciences of the United States of America - 15 Apr 1992
Privé G G, Milburn M V, Tong L, de Vos A M, Yamaizumi Z, Nishimura S, Kim S H
Abstract excerpt
RAS genes isolated from human tumors often have mutations at positions corresponding to amino acid 12 or 61 of the encoded protein (p21), while retroviral ras-encoded p21 contains substitutions at both positions 12 and 59. These mutant proteins are deficient in their GTP hydrolysis activity, and...
Topics
- Amino Acid Sequence
- Binding Sites
- Guanosine Triphosphate
- Humans
- Hydrolysis
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Proto-Oncogene Proteins p21(ras)
- X-Ray Diffraction