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

Article Details

Citation

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

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

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

PubMed ID
2476675 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
GTPase HRasP01112Details