1JH4

Solution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip1

1JH4 の概要

• エントリーDOI: 10.2210/pdb1jh4/pdb
• 関連するPDBエントリー: 1G9L 1JGN
• NMR情報: BMRB: 5084
• 分子名称: polyadenylate-binding protein 1, polyadenylate-binding protein-interacting protein-1 (2 entities in total)
• 機能のキーワード: all-helical domain, protein-peptide complex, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P11940; Cytoplasm (Probable): Q9H074
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12775.64

構造登録者

Kozlov, G.,Siddiqui, N.,Coillet-Matillon, S.,Ekiel, I.,Gehring, K. (登録日: 2001-06-27, 公開日: 2003-06-24, 最終更新日: 2024-05-22)

主引用文献

Kozlov, G.,De Crescenzo, G.,Lim, N.S.,Siddiqui, N.,Fantus, D.,Kahvejian, A.,Trempe, J.F.,Elias, D.,Ekiel, I.,Sonenberg, N.,O'Connor-McCourt, M.,Gehring, K.
Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase
EMBO J., 23:272-281, 2004

PubMed Abstract: 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.

PubMed: 14685257
DOI: 10.1038/sj.emboj.7600048

実験手法

SOLUTION NMR