Open AccessCrystallization and preliminary X‐ray diffraction analysis of the MIF4G domain of DAP5
Author(s) -
Frank Filipp,
Virgili Geneviève,
Sonenberg Nahum,
Nagar Bhushan
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109044315
Subject(s) - eif4g , crystallization , translation (biology) , eukaryotic translation , crystallography , internal ribosome entry site , computational biology , biology , chemistry , messenger rna , genetics , gene , organic chemistry
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.