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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Bibliographic Details
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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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/341209a0