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2L0T

Solution structure of the complex of ubiquitin and the VHS domain of Stam2

2L0T の概要
エントリーDOI10.2210/pdb2l0t/pdb
関連するPDBエントリー1D3Z 1X5B
分子名称Ubiquitin, Signal transducing adapter molecule 2 (2 entities in total)
機能のキーワードubiquitin, vhs, stam2, endosome, transport, protein transport
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Cytoplasm (By similarity): O75886
タンパク質・核酸の鎖数2
化学式量合計26262.05
構造登録者
Lange, A.,Hoeller, D.,Wienk, H.,Marcillat, O.,Lancelin, J.,Walker, O. (登録日: 2010-07-15, 公開日: 2010-12-15, 最終更新日: 2024-05-01)
主引用文献Lange, A.,Hoeller, D.,Wienk, H.,Marcillat, O.,Lancelin, J.M.,Walker, O.
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Biochemistry, 50:48-62, 2011
Cited by
PubMed Abstract: The VHS domain of the Stam2 protein is a ubiquitin binding domain involved in the recognition of ubiquitinated proteins committed to lysosomal degradation. Among all VHS domains, the VHS domain of Stam proteins is the strongest binder to monoubiqiuitin and exhibits preferences for K63-linked chains. In the present paper, we report the solution NMR structure of the Stam2-VHS domain in complex with monoubiquitin by means of chemical shift perturbations, spin relaxation, and paramagnetic relaxation enhancements. We also characterize the interaction of Stam2-VHS with K48- and K63-linked diubiquitin chains and report the first evidence that VHS binds differently to these two chains. Our data reveal that VHS enters the hydrophobic pocket of K48-linked diubiquitin and binds the two ubiquitin subunits with different affinities. In contrast, VHS interacts with K63-linked diubiquitin in a mode similar to its interaction with monoubiquitin. We also suggest possible structural models for both K48- and K63-linked diubiquitin in interaction with VHS. Our results, which demonstrate a different mode of binding of VHS for K48- and K63-linked diubiquitin, may explain the preference of VHS for K63- over K48-linked diubiquitin chains and monoubiquitin.
PubMed: 21121635
DOI: 10.1021/bi101594a
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 2l0t
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2026-04-22に公開中

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