title: Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.
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.
authors.affiliation: Department of Biochemistry, McGill University, Montréal, Québec, Canada.
authors.forename: Filipp
authors.initials: F
authors.lastname: Frank
authors.forename: Geneviève
authors.initials: G
authors.lastname: Virgili
authors.forename: Nahum
authors.initials: N
authors.lastname: Sonenberg
authors.forename: Bhushan
authors.initials: B
authors.lastname: Nagar
mesh_terms: D003460:Crystallization; D004926:Escherichia coli / Q000378:metabolism; D039603:Eukaryotic Initiation Factor-4G / Q000737:chemistry*; D006801:Humans; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: C491300:EIF4G2 protein, human; D039603:Eukaryotic Initiation Factor-4G; D011994:Recombinant Proteins