X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis.
Privé, G G
X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Apr 1992 - 3649-53 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
0027-8424
10.1073/pnas.89.8.3649 doi
Amino Acid Sequence
Binding Sites
Guanosine Triphosphate--metabolism
Humans
Hydrolysis
Models, Molecular
Molecular Sequence Data
Mutation
Protein Conformation
Proto-Oncogene Proteins p21(ras)--chemistry
X-Ray Diffraction--methods
X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Apr 1992 - 3649-53 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
0027-8424
10.1073/pnas.89.8.3649 doi
Amino Acid Sequence
Binding Sites
Guanosine Triphosphate--metabolism
Humans
Hydrolysis
Models, Molecular
Molecular Sequence Data
Mutation
Protein Conformation
Proto-Oncogene Proteins p21(ras)--chemistry
X-Ray Diffraction--methods