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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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Cell_62_1990_539.pdf (beliebiger Volltext), 5MB
 
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http://www.cell.com/cell/pdf/0092-8674(90)90018-A.pdf (beliebiger Volltext)
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 Urheber:
Krengel, Ute1, Autor           
Schlichting, Ilme1, 2, Autor           
Scherer, Anna3, Autor           
Schumann, Renate1, 4, Autor           
Frech, Matthias, Autor
John, Jacob, Autor
Kabsch, Wolfgang1, 3, Autor           
Pai, Emil F., Autor
Wittinghofer, Alfred1, Autor           
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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 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 1990-05-141990-06-191990-08-10
 Publikationsstatus: Erschienen
 Seiten: 10
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
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Titel: Cell
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Cambridge, Mass. : Cell Press
Seiten: - Band / Heft: 62 (3) Artikelnummer: - Start- / Endseite: 539 - 548 Identifikator: ISSN: 0092-8674
CoNE: https://pure.mpg.de/cone/journals/resource/954925463183