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4XKH

CRYSTAL STRUCTURE OF THE AIRAPL TANDEM UIMS IN COMPLEX WITH A LYS48-LINKED TRI-UBIQUITIN

4XKH の概要
エントリーDOI10.2210/pdb4xkh/pdb
分子名称Polyubiquitin-C, AN1-type zinc finger protein 2B (3 entities in total)
機能のキーワードtandem ubiquitin-interacting motifs, ubiquitin-binding, ubiquitin-binding protein
由来する生物種Bos taurus (Bovine)
詳細
細胞内の位置Cytoplasm : P0CH28
Endoplasmic reticulum: Q91X58
タンパク質・核酸の鎖数9
化学式量合計68861.78
構造登録者
Rahighi, S.,Kawasaki, M.,Stanhill, A.,Wakatsuki, S. (登録日: 2015-01-11, 公開日: 2016-02-17, 最終更新日: 2024-02-28)
主引用文献Rahighi, S.,Braunstein, I.,Ternette, N.,Kessler, B.,Kawasaki, M.,Kato, R.,Matsui, T.,Weiss, T.M.,Stanhill, A.,Wakatsuki, S.
Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin Chains.
Structure, 24:412-422, 2016
Cited by
PubMed Abstract: Lys48-linked ubiquitin chains act as the main targeting signals for protein degradation by the proteasome. Here we report selective binding of AIRAPL, a protein that associates with the proteasome upon exposure to arsenite, to Lys48-linked tri-ubiquitin chains. AIRAPL comprises two ubiquitin-interacting motifs in tandem (tUIMs) that are linked through a flexible inter-UIM region. In the complex crystal structure UIM1 binds the proximal ubiquitin, whereas UIM2 (the double-sided UIM) binds non-symmetrically to the middle and distal ubiquitin moieties on either side of the helix. Specificity of AIRAPL for Lys48-linked ubiquitin chains is determined by UIM2, and the flexible inter-UIM linker increases avidity by placing the two UIMs in an orientation that facilitates binding of the third ubiquitin to UIM1. Unlike middle and proximal ubiquitins, distal ubiquitin binds UIM2 through a novel surface, which leaves the Ile44 hydrophobic patch accessible for binding to the proteasomal ubiquitin receptors.
PubMed: 26876100
DOI: 10.1016/j.str.2015.12.017
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 4xkh
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2025-07-30に公開中

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