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  Studies on the structure and mechanism of H-ras p21

Goody, R. S., Pai, E. F., Schlichting, I., Rensland, H., Scheideg, A., Franken, S., et al. (1992). Studies on the structure and mechanism of H-ras p21. Philosophical Transactions of the Royal Society of London, Series B: Biological Sciences, 336(1276), 3-11. doi:10.1098/rstb.1992.0037.

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 Creators:
Goody, Roger S.1, Author              
Pai, Emil F.1, Author              
Schlichting, Ilme1, 2, Author              
Rensland, Hans, Author
Scheideg, Axel, Author
Franken, Sybille1, Author              
Wittinghofer, Alfred1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society, ou_1856341              

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 Abstract: Current knowledge of the structure of H-ras p21 is reviewed with particular emphasis on the interaction between guanine nucleotides and the active site of the protein. The nature of the conformational change induced by GTP hydrolysis is discussed. The major change is seen in the region known as the effector loop (loop 2), with significant but less well-defined changes occurring in loop 4, which is implicated in the GTPase reaction. Other evidence concerning the mechanism of GTP hydrolysis and its activation by GAP (GTPase-activating protein) is also discussed. Evidence regarding the rate limiting step in the p21 GTPase reaction, and the manner in which this and possibly other steps are accelerated by GAP, is inconclusive.

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Language(s): eng - English
 Dates: 1992-04-29
 Publication Status: Published in print
 Pages: 9
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 Rev. Type: Peer
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Title: Philosophical Transactions of the Royal Society of London, Series B: Biological Sciences
Source Genre: Journal
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Publ. Info: London : Royal Society
Pages: - Volume / Issue: 336 (1276) Sequence Number: - Start / End Page: 3 - 11 Identifier: ISSN: 0962-8436
CoNE: https://pure.mpg.de/cone/journals/resource/963017382021_1