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Crystallization and preliminary X-ray diffraction analysis of the middle domain of Paip1.

ABSTRACT: The poly(A)-binding protein (PABP) simultaneously interacts with the poly(A) tail of mRNAs and the scaffolding protein eIF4G to mediate mRNA circularization, resulting in stimulation of protein translation. PABP is regulated by the PABP-interacting protein Paip1. Paip1 is thought to act as a translational activator in 5' cap-dependent translation by interacting with PABP and the initiation factors eIF4A and eIF3. Here, the crystallization and preliminary diffraction analysis of the middle domain of Paip1 (Paip1M), which produces crystals that diffract to a resolution of 2.2 A, are presented.

SUBMITTER: Kanaan AS

PROVIDER: S-EPMC2765901 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the middle domain of Paip1.

Kanaan Ahmad Seif AS Frank Filipp F Maedler-Kron Chelsea C Verma Karan K Sonenberg Nahum N Nagar Bhushan B

Acta crystallographica. Section F, Structural biology and crystallization communications 20090925 Pt 10

The poly(A)-binding protein (PABP) simultaneously interacts with the poly(A) tail of mRNAs and the scaffolding protein eIF4G to mediate mRNA circularization, resulting in stimulation of protein translation. PABP is regulated by the PABP-interacting protein Paip1. Paip1 is thought to act as a translational activator in 5' cap-dependent translation by interacting with PABP and the initiation factors eIF4A and eIF3. Here, the crystallization and preliminary diffraction analysis of the middle domain ...[more]

PMID: 19851022

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