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. 1991 Jun;93:11–15. doi: 10.1289/ehp.919311

Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.

F Wittinghofer 1, U Krengel 1, J John 1, W Kabsch 1, E F Pai 1
PMCID: PMC1568068  PMID: 1773783

Abstract

The three-dimensional structure of the active guanosine triphosphate (GTP)-analogue-containing complex of the H-ras-encoded p21 has been determined. It was necessary to correct the topology of p21 as published earlier. The structure analysis shows all of the interactions between protein and GTP and how the important cofactor Mg2+ is bound. From the oncogenic mutants of p21 crystallized, a Gly12 to Arg mutation has been analyzed in detail. It shows that the overall structure of the mutant is not perturbed and that the side chain of Arg12 is coming close to the gamma-phosphate for an interaction.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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