Unknown

Dataset Information

0

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.

SUBMITTER: Frank F 

PROVIDER: S-EPMC2805526 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Frank Filipp F   Virgili Geneviève G   Sonenberg Nahum N   Nagar Bhushan B  

Acta crystallographica. Section F, Structural biology and crystallization communications 20091225 Pt 1


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 p  ...[more]

Similar Datasets

| S-EPMC2765901 | biostudies-literature
| S-EPMC3659266 | biostudies-literature
| S-EPMC3758161 | biostudies-literature
| S-EPMC2374246 | biostudies-literature
| S-EPMC3976062 | biostudies-literature
| S-EPMC2330201 | biostudies-literature
| S-EPMC2935245 | biostudies-literature
| S-EPMC3515377 | biostudies-literature
| S-EPMC2374253 | biostudies-literature
| S-EPMC2705634 | biostudies-literature