3KTR

Structural basis of ataxin-2 recognition by poly(A)-binding protein

3KTR の概要

• エントリーDOI: 10.2210/pdb3ktr/pdb
• 関連するPDBエントリー: 3KTP
• 分子名称: Polyadenylate-binding protein 1, Ataxin-2, CADMIUM ION, ... (5 entities in total)
• 機能のキーワード: protein-protein complex, acetylation, alternative splicing, cytoplasm, methylation, mrna processing, mrna splicing, nucleus, phosphoprotein, rna-binding, spliceosome, neurodegeneration, parkinsonism, polymorphism, spinocerebellar ataxia, triplet repeat expansion, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P11940; Cytoplasm (By similarity): Q99700
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 11665.54

構造登録者

Kozlov, G.,Gehring, K. (登録日: 2009-11-25, 公開日: 2010-02-23, 最終更新日: 2023-09-06)

主引用文献

Kozlov, G.,Safaee, N.,Rosenauer, A.,Gehring, K.
Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein.
J.Biol.Chem., 285:13599-13606, 2010

PubMed Abstract: Poly(A)-binding protein (PABPC1) is involved in multiple aspects of mRNA processing and translation. It is a component of RNA stress granules and binds the RNA-induced silencing complex to promote degradation of silenced mRNAs. Here, we report the crystal structures of the C-terminal Mlle (or PABC) domain in complex with peptides from GW182 (TNRC6C) and Ataxin-2. The structures reveal overlapping binding sites but with unexpected diversity in the peptide conformation and residues involved in binding. The mutagenesis and binding studies show low to submicromolar binding affinity with overlapping but distinct specificity determinants. These results rationalize the role of the Mlle domain of PABPC1 in microRNA-mediated mRNA deadenylation and suggest a more general function in the assembly of cytoplasmic RNA granules.

PubMed: 20181956
DOI: 10.1074/jbc.M109.089540

実験手法

X-RAY DIFFRACTION (1.7 Å)