摘要：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. Full text Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (910K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References . 11 12 13 14 15
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