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2GPQ

Cap-free structure of eIF4E suggests basis for its allosteric regulation

2GPQ の概要
エントリーDOI10.2210/pdb2gpq/pdb
分子名称Eukaryotic translation initiation factor 4E (1 entity in total)
機能のキーワードtranslation regulation, eif4e, apo form, translation
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数1
化学式量合計25130.24
構造登録者
Volpon, L.,Osborne, M.J.,Borden, K.L.B. (登録日: 2006-04-18, 公開日: 2006-11-14, 最終更新日: 2024-05-29)
主引用文献Volpon, L.,Osborne, M.J.,Topisirovic, I.,Siddiqui, N.,Borden, K.L.
Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands.
Embo J., 25:5138-5149, 2006
Cited by
PubMed Abstract: The activity of the eukaryotic translation initiation factor eIF4E is modulated through conformational response to its ligands. For example, eIF4G and eIF4E-binding proteins (4E-BPs) modulate cap affinity, and thus physiological activity of eIF4E, by binding a site distal to the 7-methylguanosine cap-binding site. Further, cap binding substantially modulates eIF4E's affinity for eIF4G and the 4E-BPs. To date, only cap-bound eIF4E structures were reported. In the absence of structural information on the apo form, the molecular underpinnings of this conformational response mechanism cannot be established. We report here the first cap-free eIF4E structure. Apo-eIF4E exhibits structural differences in the cap-binding site and dorsal surface relative to cap-eIF4E. Analysis of structure and dynamics of apo-eIF4E, and changes observed upon ligand binding, reveal a molecular basis for eIF4E's conformational response to these ligands. In particular, alterations in the S4-H4 loop, distal to either the cap or eIF4G binding sites, appear key to modulating these effects. Mutation in this loop mimics these effects. Overall, our studies have important implications for the regulation of eIF4E.
PubMed: 17036047
DOI: 10.1038/sj.emboj.7601380
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2gpq
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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