3rk6

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Template:STRUCTURE 3rk6

Contents 1 Crystal structure of the middle domain of human Paip1 2 Function 3 About this Structure 4 Reference

Crystal structure of the middle domain of human Paip1

Template:ABSTRACT PUBMED 21539810

Function

[PAIP1_HUMAN] Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain.^{[1] [2]}

About this Structure

3rk6 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

• Lei J, Mesters JR, Brunn AV, Hilgenfeld R. Crystal structure of the middle domain of human poly(A)-binding protein-interacting protein 1. Biochem Biophys Res Commun. 2011 Apr 23. PMID:21539810 doi:10.1016/j.bbrc.2011.04.088

1. ↑ Craig AW, Haghighat A, Yu AT, Sonenberg N. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature. 1998 Apr 2;392(6675):520-3. PMID:9548260 doi:10.1038/33198
2. ↑ Grosset C, Chen CY, Xu N, Sonenberg N, Jacquemin-Sablon H, Shyu AB. A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell. 2000 Sep 29;103(1):29-40. PMID:11051545