Nature. 1989 Sep 21;341(6239):209-14.

Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation.

Pai EF, Kabsch W, Krengel U, Holmes KC, John J, Wittinghofer A.

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Max-Planck-Institut für medizinische Forschung, Abteilung Biophysik, Heidelberg, FRG.

Abstract

The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1-166) complexed to the guanosine triphosphate analogue guanosine-5'-(beta, gamma-imido)triphosphate (GppNp) has been determined at a resolution of 2.6 A. The topological order of secondary structure elements is the same as that of the guanine-nucleotide-binding domain of bacterial elongation factor EF-Tu. Many interactions between nucleotide and protein have been identified. The effects of point mutations and the conservation of amino-acid sequence in the guanine-nucleotide-binding proteins are discussed.

PMID:: 2476675; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Refined Crystal Structure Of The Triphosphate Conformation Of H-Ras P21 At 1.35 Angstroms Resolution: Implications For The Mechanism Of Gtp Hydrolysis

PDB: 5P21

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 1.35 Å

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Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation.

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