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Science 4 October 1985:
Vol. 230. no. 4721, pp. 78 - 82
DOI: 10.1126/science.3898366
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Articles

Science, Vol 230, Issue 4721, 78-82
Copyright © 1985 by American Association for the Advancement of Science

articles

A model for the tertiary structure of p21, the product of the ras oncogene

F McCormick, BF Clark, TF la Cour, M Kjeldgaard, L Norskov-Lauritsen, and J Nyborg

A model was developed for the structure of p21, the protein with a molecular weight of 21,000 that is produced by the ras genes. This model predicts that p21 consists of a central core of beta-sheet structure, connected by loops and alpha helices. Four of these loops comprise the guanine nucleotide binding site. The phosphoryl binding region is made up of amino acid sequences from 10 to 16 and from 57 to 63 of p21. The latter sequence may contain a site for magnesium binding. Amino acids defining guanine specificity are Asn-116 and Asp-119, and sequences around amino acid 145 may contribute to guanine binding. The model makes it possible to visualize how oncogenic mutations of p21 affect interaction with guanine nucleotides.


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Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21.
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ras Oncogene Proteins: Three-dimensional Structures, Functional Implications, and a Model for Signal Transducer.
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A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)