Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling

Nat Struct Biol. 1997 Sep;4(9):694-9. doi: 10.1038/nsb0997-694.

Abstract

The solution structure of the Ras-binding domain (RBD) of Ral guanine-nucleotide exchange factor RalGEF was solved by NMR spectroscopy. The overall structure is similar to that of Raf-RBD, another effector of Ras, although the sequence identity is only 13%. 15N chemical shifts changes in the complex of RalGEF-RBD with Ras indicate an interaction similar to the intermolecular beta-sheet observed for the complex between Ras and Raf-RBD.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • GTP-Binding Proteins / chemistry*
  • Humans
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Signal Transduction / physiology*
  • rap GTP-Binding Proteins
  • ras Proteins / chemistry*

Substances

  • GTP-Binding Proteins
  • rap GTP-Binding Proteins
  • ras Proteins

Associated data

  • GENBANK/U14417