Structure of the GDP-bound G domain of the RGK protein Rem2

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):626-31. doi: 10.1107/S1744309112013541. Epub 2012 May 22.


RGK proteins are atypical small GTP-binding proteins that are involved in the regulation of voltage-dependent calcium channels and actin cytoskeleton remodelling. The structure of the Rem2 G domain bound to GDP is reported here in a monoclinic crystal form at 2.66 Å resolution. It is very similar to the structure determined previously from an orthorhombic crystal form. However, differences in the crystal-packing environment revealed that the switch I and switch II regions are flexible and not ordered as previously reported. Comparison of the available RGK protein structures along with those of other small GTP-binding proteins highlights two structural features characteristic of this atypical family and suggests that the conserved tryptophan residue in the DXWEX motif may be a structural determinant of the nucleotide-binding affinity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Guanosine Diphosphate
  • Models, Molecular
  • Molecular Sequence Data
  • Monomeric GTP-Binding Proteins / chemistry*
  • Monomeric GTP-Binding Proteins / metabolism
  • Protein Interaction Domains and Motifs*
  • Protein Structure, Tertiary
  • Rats
  • Sequence Alignment


  • Guanosine Diphosphate
  • Monomeric GTP-Binding Proteins
  • Rem2 protein, rat

Associated data

  • PDB/4AII