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1jgn

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Revision as of 15:34, 12 November 2007


1jgn

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Solution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip2

Overview

The C-terminal domain of poly(A)-binding protein (PABC) is a, peptide-binding domain found in poly(A)-binding proteins (PABPs) and a, HECT (homologous to E6-AP C-terminus) family E3 ubiquitin ligase. In, protein synthesis, the PABC domain of PABP functions to recruit several, translation factors possessing the PABP-interacting motif 2 (PAM2) to the, mRNA poly(A) tail. We have determined the solution structure of the human, PABC domain in complex with two peptides from PABP-interacting protein-1, (Paip1) and Paip2. The structures show a novel mode of peptide, recognition, in which the peptide binds as a pair of beta-turns with, extensive hydrophobic, electrostatic and aromatic stacking interactions., Mutagenesis of PABC and peptide residues was used to identify key, protein-peptide interactions and quantified by isothermal calorimetry, surface plasmon resonance and GST pull-down assays. The results provide, insight into the specificity of PABC in mediating PABP-protein, interactions.

About this Structure

1JGN is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase., Kozlov G, De Crescenzo G, Lim NS, Siddiqui N, Fantus D, Kahvejian A, Trempe JF, Elias D, Ekiel I, Sonenberg N, O'Connor-McCourt M, Gehring K, EMBO J. 2004 Jan 28;23(2):272-81. Epub 2003 Dec 18. PMID:14685257

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