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PMID: 2476675 Published · ppublish English Journal Article

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

Nature ·Vol. 341 ·No. 6239 ·1989-09-21 ·Pages 209-14

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

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.

MeSH Terms
Binding Sites Computer Graphics Crystallography Epitopes GTP Phosphohydrolases GTP-Binding Proteins/immunology,ultrastructure Guanylyl Imidodiphosphate Humans Magnesium Phosphates Protein Conformation Proto-Oncogene Proteins/immunology,ultrastructure Proto-Oncogene Proteins p21(ras)
Chemicals
Epitopes Phosphates Proto-Oncogene Proteins Guanylyl Imidodiphosphate GTP Phosphohydrolases GTP-Binding Proteins HRAS protein, human Proto-Oncogene Proteins p21(ras) Magnesium
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Pai E F
Max-Planck-Institut für medizinische Forschung, Abteilung Biophysik, Heidelberg, FRG.
Kabsch W
Krengel U
Holmes K C
John J
Wittinghofer A
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1989-09-21
Pages
209-14
Language
English
Region
England
NLM ID
0410462
Subset
IM
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