3KUS

Crystal structure of the MLLE domain of poly(A)-binding protein in complex with the binding region of Paip2

3KUS の概要

• エントリーDOI: 10.2210/pdb3kus/pdb
• 関連するPDBエントリー: 3KUR 3KUT
• 分子名称: Polyadenylate-binding protein 1, PAIP2 protein, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: protein-protein complex, methylation, mrna processing, mrna splicing, nucleus, phosphoprotein, rna-binding, spliceosome, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P11940
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 22405.87

構造登録者

Kozlov, G.,Gehring, K. (登録日: 2009-11-27, 公開日: 2010-02-09, 最終更新日: 2023-09-06)

主引用文献

Kozlov, G.,Menade, M.,Rosenauer, A.,Nguyen, L.,Gehring, K.
Molecular Determinants of PAM2 Recognition by the MLLE Domain of Poly(A)-Binding Protein.
J.Mol.Biol., 397:397-407, 2010

PubMed Abstract: MLLE (previously known as PABC) is a peptide-binding domain that is found in poly(A)-binding protein (PABP) and EDD (E3 isolated by differential display), a HECT E3 ubiquitin ligase also known as HYD (hyperplastic discs tumor suppressor) or UBR5. The MLLE domain from PABP recruits various regulatory proteins and translation factors to poly(A) mRNAs through binding of a conserved 12 amino acid peptide motif called PAM2 (for PABP-interacting motif 2). Here, we determined crystal structures of the MLLE domain from PABP alone and in complex with PAM2 peptides from PABP-interacting protein 2. The structures provide a detailed view of hydrophobic determinants of the MLLE binding coded by PAM2 positions 3, 5, 7, 10, and 12 and reveal novel intermolecular polar contacts. In particular, the side chain of the invariant MLLE residue K580 forms hydrogen bonds with the backbone of PAM2 residues 5 and 7. The structures also show that peptide residues outside of the conserved PAM2 motif contribute to binding. Altogether, the structures provide a significant advance in understanding the molecular basis for the binding of PABP by PAM2-containing proteins involved in translational control, mRNA deadenylation, and other cellular processes.

PubMed: 20096703
DOI: 10.1016/j.jmb.2010.01.032

実験手法

X-RAY DIFFRACTION (1.4 Å)