Three-dimensional structure of the Ras-interacting domain of RalGDS

Nat Struct Biol. 1997 Aug;4(8):609-15. doi: 10.1038/nsb0897-609.

Abstract

The Ras-interacting domains of the the protein-kinase Raf and the Ral guanine nucleotide dissociation stimulator, RalGDS, lack extensive sequence similarity, but their overall three-dimensional structures are very similar to each other. Mutational analysis indicated that three residues in the RalGDS domain are critical for its interaction with Ras.

Publication types

  • Comparative Study
  • Letter
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • DNA Mutational Analysis
  • GTP-Binding Proteins / chemistry*
  • GTP-Binding Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Protein Serine-Threonine Kinases / chemistry
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Structure, Secondary
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-raf
  • Proto-Oncogene Proteins p21(ras) / chemistry*
  • Proto-Oncogene Proteins p21(ras) / metabolism
  • Sequence Alignment
  • Ubiquitins / chemistry
  • ral Guanine Nucleotide Exchange Factor
  • rap GTP-Binding Proteins

Substances

  • Peptide Fragments
  • Proto-Oncogene Proteins
  • Ubiquitins
  • ral Guanine Nucleotide Exchange Factor
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-raf
  • GTP-Binding Proteins
  • Proto-Oncogene Proteins p21(ras)
  • rap GTP-Binding Proteins