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

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...

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Published in:	Nature (London) 1989-09, Vol.341 (6239), p.209-214
Main Authors:	Pai, Emil F, Kabsch, Wolfgang, Krengel, Ute, Holmes, Kenneth C, John, Jacob, Wittinghofer, Alfred
Format:	Article
Language:	English
Subjects:	Acids Amino acids Binding Sites Biochemistry Biological and medical sciences Computer Graphics Crystallography Epitopes Fundamental and applied biological sciences. Psychology GTP Phosphohydrolases GTP-Binding Proteins - immunology GTP-Binding Proteins - ultrastructure Guanylyl Imidodiphosphate Humans Interactions. Associations Intermolecular phenomena Magnesium Molecular biophysics Mutation Phosphates Protein Conformation Proteins Proto-Oncogene Proteins - immunology Proto-Oncogene Proteins - ultrastructure Proto-Oncogene Proteins p21(ras)
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creator	Pai, Emil F Kabsch, Wolfgang Krengel, Ute Holmes, Kenneth C John, Jacob Wittinghofer, Alfred
description	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.
doi_str_mv	10.1038/341209a0
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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.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/341209a0</identifier><identifier>PMID: 2476675</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Acids ; Amino acids ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Computer Graphics ; Crystallography ; Epitopes ; Fundamental and applied biological sciences. Psychology ; GTP Phosphohydrolases ; GTP-Binding Proteins - immunology ; GTP-Binding Proteins - ultrastructure ; Guanylyl Imidodiphosphate ; Humans ; Interactions. 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subjects	Acids Amino acids Binding Sites Biochemistry Biological and medical sciences Computer Graphics Crystallography Epitopes Fundamental and applied biological sciences. Psychology GTP Phosphohydrolases GTP-Binding Proteins - immunology GTP-Binding Proteins - ultrastructure Guanylyl Imidodiphosphate Humans Interactions. Associations Intermolecular phenomena Magnesium Molecular biophysics Mutation Phosphates Protein Conformation Proteins Proto-Oncogene Proteins - immunology Proto-Oncogene Proteins - ultrastructure Proto-Oncogene Proteins p21(ras)
title	Structure of the guanine-nucleotide-binding domain of the Ha- ras oncogene product p21 in the triphosphate conformation
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