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Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis
Open accessAbstract
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.
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Citations
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Metadata
- Authors
- Schlichting, I., Almo, S. C., Rapp, G., Wilson, K., Petratos, K., Lentfer, A., Wittinghofer, A., Kabsch, W., Pai, E. F., Petsko, G. A., & Goody, R. S.
- Venue
- Nature
- Published
- 1990-05
- Volume
- 345
- Issue
- 6273
- Pages
- 309-315
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2078668386
- Cited by
- 487
- References
- 0
- FWCI
- 19.18
- Type
- journal article
- Language
- en
- Open access
- green
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