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

Fred Wittinghofer | Zendy; Ute Krengel | Zendy; John J. Sauk | Zendy; Wolfgang Kabsch | Zendy; E.F. Pai | Zendy

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

Author(s) -

Fred Wittinghofer,

Ute Krengel,

John J. Sauk,

Wolfgang Kabsch,

E.F. Pai

Publication year - 1991

Publication title -

environmental health perspectives

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.257

H-Index - 282

eISSN - 1552-9924

pISSN - 0091-6765

DOI - 10.1289/ehp.919311

Subject(s) - mutant , gtp' , guanosine , guanosine triphosphate , mutation , chemistry , protein structure , biology , topology (electrical circuits) , crystallography , biochemistry , gene , enzyme , mathematics , combinatorics

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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