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4GML

Crystal structure of human NOT1 MIF4G domain

4GML の概要
エントリーDOI10.2210/pdb4gml/pdb
分子名称CCR4-NOT transcription complex subunit 1 (2 entities in total)
機能のキーワードccr4-not, deadenylation, mrna decay, deadenylase, transcription, rna binding protein
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm, P-body (By similarity): A5YKK6
タンパク質・核酸の鎖数6
化学式量合計163624.43
構造登録者
Petit, P.,Weichenrieder, O.,Wohlbold, L.,Izaurralde, E. (登録日: 2012-08-16, 公開日: 2012-10-03, 最終更新日: 2023-11-08)
主引用文献Petit, A.P.,Wohlbold, L.,Bawankar, P.,Huntzinger, E.,Schmidt, S.,Izaurralde, E.,Weichenrieder, O.
The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex
Nucleic Acids Res., 40:11058-11072, 2012
Cited by
PubMed Abstract: The CCR4-NOT complex plays a crucial role in post-transcriptional mRNA regulation in eukaryotic cells. It catalyzes the removal of mRNA poly(A) tails, thereby repressing translation and committing mRNAs to decay. The conserved core of the complex consists of a catalytic module comprising two deadenylases (CAF1/POP2 and CCR4a/b) and the NOT module, which contains at least NOT1, NOT2 and NOT3. NOT1 bridges the interaction between the two modules and therefore, acts as a scaffold protein for the assembly of the complex. Here, we present the crystal structures of the CAF1-binding domain of human NOT1 alone and in complex with CAF1. The NOT1 domain comprises five helical hairpins that adopt an MIF4G (middle portion of eIF4G) fold. This NOT1 MIF4G domain binds CAF1 through a pre-formed interface and leaves the CAF1 catalytic site fully accessible to RNA substrates. The conservation of critical structural and interface residues suggests that the NOT1 MIF4G domain adopts a similar fold and interacts with CAF1 in a similar manner in all eukaryotes. Our findings shed light on the assembly of the CCR4-NOT complex and provide the basis for dissecting the role of the NOT module in mRNA deadenylation.
PubMed: 22977175
DOI: 10.1093/nar/gks883
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 4gml
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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