4C0E

Structure of the NOT1 superfamily homology domain from Chaetomium thermophilum

4C0E の概要

• エントリーDOI: 10.2210/pdb4c0e/pdb
• 関連するPDBエントリー: 4C0D 4C0F 4C0G
• 分子名称: NOT1 (1 entity in total)
• 機能のキーワード: gene regulation, deadenylation, mrna decay, ccr4-not, hydrolase, transcription
• 由来する生物種: CHAETOMIUM THERMOPHILUM
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 239932.42

構造登録者

Chen, Y.,Boland, A.,Raisch, T.,Jonas, S.,Izaurralde, E.,Weichenrieder, O. (登録日: 2013-08-01, 公開日: 2013-10-09, 最終更新日: 2024-11-06)

主引用文献

Boland, A.,Chen, Y.,Raisch, T.,Jonas, S.,Kuzuoglu-Ozturk, D.,Wohlbold, L.,Weichenrieder, O.,Izaurralde, E.
Structure and Assembly of the not Module of the Human Ccr4-not Complex
Nat.Struct.Mol.Biol., 20:1289-, 2013

PubMed Abstract: The CCR4-NOT deadenylase complex is a master regulator of translation and mRNA stability. Its NOT module orchestrates recruitment of the catalytic subunits to target mRNAs. We report the crystal structure of the human NOT module formed by the CNOT1, CNOT2 and CNOT3 C-terminal (-C) regions. CNOT1-C provides a rigid scaffold consisting of two perpendicular stacks of HEAT-like repeats. CNOT2-C and CNOT3-C heterodimerize through their SH3-like NOT-box domains. The heterodimer is stabilized and tightly anchored to the surface of CNOT1 through an unexpected intertwined arrangement of peptide regions lacking defined secondary structure. These assembly peptides mold onto their respective binding surfaces and form extensive interfaces. Mutagenesis of individual interfaces and perturbation of endogenous protein ratios cause defects in complex assembly and mRNA decay. Our studies provide a structural framework for understanding the recruitment of the CCR4-NOT complex to mRNA targets.

PubMed: 24121232
DOI: 10.1038/NSMB.2681

実験手法

X-RAY DIFFRACTION (3.2 Å)