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Crystal structure of the middle domain of human poly(A)-binding protein-interacting protein 1.

Lei J, Mesters JR, von Brunn A, Hilgenfeld R
Biochem Biophys Res Commun 408 680-5 (2011)
Cited: 6 times
EuropePMC logo PMID: 21539810

Abstract

In eukaryotes, the poly(A)-binding protein (PABP) is one of the important factors for initiation of messenger RNA translation. PABP activity is regulated by the PABP-interacting proteins (Paips), which include Paip1, Paip2A, and Paip2B. Human Paip1 has three different isoforms. Here, we report the crystal structure of the middle domain of Paip1 isoform 2 (Paip1M) as determined by single-wavelength anomalous dispersion phasing. The structure reveals a crescent-shaped domain consisting of 10 α-helices and two antiparallel β-strands forming a β-hairpin. The 10 α-helices are arranged as five HEAT repeats which form a double layer of α helices with a convex and a concave surface. Despite low sequence identity, the overall fold of Paip1M is similar to the middle domain of human eIF4GII and yeast eIF4GI. Moreover, the amino-acid sequence motif and the local structure of eIF4G involved in binding of eIF4A, are conserved in Paip1. The structure reported here is the first of a member of the Paip family, thereby filling a gap in our understanding of initiation of eukaryotic mRNA translation in three dimensions.

Articles - 3rk6 mentioned but not cited (3)

  1. The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation. Lei J, Ma-Lauer Y, Han Y, Thoms M, Buschauer R, Jores J, Thiel V, Beckmann R, Deng W, Leonhardt H, Hilgenfeld R, von Brunn A. EMBO J 40 e102277 (2021)
  2. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)
  3. Crystal structure of the MIF4G domain of the Trypanosoma cruzi translation initiation factor EIF4G5. Camillo Dos Santos LP, de Matos BM, de Maman Ribeiro BC, Zanchin NIT, Guimarães BG. Acta Crystallogr F Struct Biol Commun 75 738-743 (2019)


Articles citing this publication (3)

  1. The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex. Petit AP, Wohlbold L, Bawankar P, Huntzinger E, Schmidt S, Izaurralde E, Weichenrieder O. Nucleic Acids Res 40 11058-11072 (2012)
  2. Structural basis of SOSS1 complex assembly and recognition of ssDNA. Ren W, Chen H, Sun Q, Tang X, Lim SC, Huang J, Song H. Cell Rep 6 982-991 (2014)
  3. Novel roles of the CCR4-NOT complex. Chapat C, Corbo L. Wiley Interdiscip Rev RNA 5 883-901 (2014)


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