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DOI | 10.2210/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: 26876100DOI: 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) |
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