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

Abstract

The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1–166) complexed to the guanosine triphosphate analogue guanosine-5′-(β, γ-imido)triphosphate (GppNp) has been determined at a resolution of 2.6 Å. 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.

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Pai, E., Kabsch, W., Krengel, U. et al. Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341, 209–214 (1989). https://doi.org/10.1038/341209a0

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