Literature DB >> 2476675

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

E F Pai1, W Kabsch, U Krengel, K C Holmes, J John, A Wittinghofer.   

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.

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Year:  1989        PMID: 2476675     DOI: 10.1038/341209a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  220 in total

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5.  Complementation of sporulation and motility defects in a prokaryote by a eukaryotic GTPase.

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Journal:  Proc Natl Acad Sci U S A       Date:  1997-09-02       Impact factor: 11.205

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Authors:  S Hsieh; D A Julin
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Journal:  Mol Cell Biol       Date:  1992-04       Impact factor: 4.272

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10.  The structure of the carboxyl terminus of the p21 protein. Structural relationship to the nucleotide-binding/transforming regions of the protein.

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Journal:  J Protein Chem       Date:  1990-04
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