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

Nature. 1989 Sep 21;341(6239):209-14. doi: 10.1038/341209a0.

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
  • GTP-Binding Proteins / ultrastructure*
  • Guanylyl Imidodiphosphate
  • Humans
  • Magnesium
  • Phosphates
  • Protein Conformation
  • Proto-Oncogene Proteins / immunology
  • Proto-Oncogene Proteins / ultrastructure*
  • Proto-Oncogene Proteins p21(ras)

Substances

  • Epitopes
  • Phosphates
  • Proto-Oncogene Proteins
  • Guanylyl Imidodiphosphate
  • GTP Phosphohydrolases
  • GTP-Binding Proteins
  • HRAS protein, human
  • Proto-Oncogene Proteins p21(ras)
  • Magnesium