| Autor: |
Brünger, A T, Milburn, M V, Tong, L, deVos, A M, Jancarik, J, Yamaizumi, Z, Nishimura, S, Ohtsuka, E, Kim, S H |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; June 1990, Vol. 87 Issue: 12 p4849-4853, 5p |
| Abstrakt: |
Normal RAS proteins play a key role of molecular switch in the transduction of the growth signal from extracellular to intracellular space. The state of the switch is "on" when GTP is bound and "off" when GDP is bound to the protein. The crystal structure of a complex between a nonhydrolyzable GTP analog and the catalytic domain of a RAS protein has been determined by a rotation-translation search method. The orientations and positions of four independent molecules have been determined using a single molecule as a probe in the search. The crystal structure reveals that the gamma phosphate of the GTP analog induces extensive conformational changes on two loop regions of the protein. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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