Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):15-9. doi: 10.1107/S1744309109044315. Epub 2009 Dec 25.

Abstract

Death-associated protein 5 (DAP5) is a member of the eIF4G family of scaffolding proteins that mediate cap-independent translation initiation by recruiting the translational machinery to internal ribosomal entry sites (IRESs) on mRNA. The MIF4G domain of DAP5 directly interacts with the eukaryotic initiation factors eIF4A and eIF3 and enhances the translation of several viral and cellular IRESs. Here, the crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5 is presented.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Escherichia coli / metabolism
  • Eukaryotic Initiation Factor-4G / chemistry*
  • Humans
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • X-Ray Diffraction

Substances

  • EIF4G2 protein, human
  • Eukaryotic Initiation Factor-4G
  • Recombinant Proteins