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  Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules

Krengel, U., Schlichting, I., Scherer, A., Schumann, R., Frech, M., John, J., et al. (1990). Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules. Cell, 62(3), 539-548. doi:10.1016/0092-8674(90)90018-A.

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Krengel, Ute1, Author              
Schlichting, Ilme1, 2, Author              
Scherer, Anna3, Author              
Schumann, Renate1, 4, Author              
Frech, Matthias, Author
John, Jacob, Author
Kabsch, Wolfgang1, 3, Author              
Pai, Emil F., 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              
3Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
4Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497708              

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 Abstract: The X-ray structures of the guanine nucleotide binding domains (amino acids 1-166) of five mutants of the H-ras oncogene product p21 were determined. The mutations described are Gly-12----Arg, Gly-12----Val, Gln-61----His, Gln-61----Leu, which are all oncogenic, and the effector region mutant Asp-38----Glu. The resolutions of the crystal structures range from 2.0 to 2.6 A. Cellular and mutant p21 proteins are almost identical, and the only significant differences are seen in loop L4 and in the vicinity of the gamma-phosphate. For the Gly-12 mutants the larger side chains interfere with GTP binding and/or hydrolysis. Gln-61 in cellular p21 adopts a conformation where it is able to catalyze GTP hydrolysis. This conformation has not been found for the mutants of Gln-61. Furthermore, Leu-61 cannot activate the nucleophilic water because of the chemical nature of its side chain. The D38E mutation preserves its ability to bind GAP.

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Language(s): eng - English
 Dates: 1990-05-141990-06-191990-08-10
 Publication Status: Published in print
 Pages: 10
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 Rev. Type: Peer
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Title: Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 62 (3) Sequence Number: - Start / End Page: 539 - 548 Identifier: ISSN: 0092-8674
CoNE: https://pure.mpg.de/cone/journals/resource/954925463183