Ontology highlight
ABSTRACT:
SUBMITTER: Hall BE
PROVIDER: S-EPMC129411 | biostudies-literature | 2002 Sep
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20020904 19
The conformational changes in Ras that accompany the hydrolysis of GTP are critical to its function as a molecular switch in signaling pathways. Understanding how GTP is hydrolyzed by revealing the sequence of intermediary structures in the reaction is essential for understanding Ras signaling. Until now, no structure of an intermediate in GTP hydrolysis has been experimentally determined for Ras alone. We have solved the crystal structure of the Ala-59 to Gly mutant of Ras, (RasA59G), bound to ...[more]