Crystal structure of the Rasputin NTF2-like domain from Drosophila melanogaster

Biochem Biophys Res Commun. 2012 Mar 30;420(1):188-92. doi: 10.1016/j.bbrc.2012.02.140. Epub 2012 Mar 3.

Abstract

The crystal structure of the NTF2-like domain of the Drosophila homolog of Ras GTPase SH3 Binding Protein (G3BP), Rasputin, was determined at 2.7Å resolution. The overall structure is highly similar to nuclear transport factor 2: It is a homodimer comprised of a β-sheet and three α-helices forming a cone-like shape. However, known binding sites for RanGDP and FxFG containing peptides show electrostatic and steric differences compared to nuclear transport factor 2. A HEPES molecule bound in the structure suggests a new, and possibly physiologically relevant, ligand binding site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Crystallography, X-Ray
  • Drosophila Proteins / chemistry*
  • Drosophila Proteins / genetics
  • HEPES / chemistry
  • Molecular Sequence Data
  • Nucleocytoplasmic Transport Proteins / chemistry*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary

Substances

  • Carrier Proteins
  • Drosophila Proteins
  • Ntf-2 protein, Drosophila
  • Nucleocytoplasmic Transport Proteins
  • rin protein, Drosophila
  • HEPES