Abstract
Crystals of Ha-Ras p21 with caged GTP at the active site have been used to investigate the conformational changes of p21 on GTP hydrolysis. The structure of the short-lived p21-GTP complex was determined by Laue diffraction methods. After GTP hydrolysis, substantial structural changes occur in the parts of the molecule implicated in the interaction with GTPase-activating protein. The trigger for this process seems to be a change in coordination of the active-site Mg2+ion as a result of loss of the γ-phosphate of GTP.
Original language | English (US) |
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Pages (from-to) | 309-315 |
Number of pages | 7 |
Journal | Nature |
Volume | 345 |
Issue number | 6273 |
DOIs | |
State | Published - 1990 |
Externally published | Yes |
ASJC Scopus subject areas
- General