2JF5

crystal structure of Lys63-linked di-ubiquitin

2JF5 の概要

• エントリーDOI: 10.2210/pdb2jf5/pdb
• 関連するPDBエントリー: 1C3T 1D3Z 1F9J 1FXT 1G6J 1GJZ 1NBF 1OGW 1Q5W 1S1Q 1SIF 1TBE 1UBI 1UBQ 1XD3 1XQQ 1YX5 1YX6 1ZGU 2AYO 2BGF 2FCM 2FCN 2FCQ 2FCS 2FUH 2G45 2GBK 2GBM 2GBN 2J7Q
• 分子名称: UBIQUITIN, CADMIUM ION, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: lys6, lys63, nf-kb, ubiquitin, nuclear protein, signal transduction, signaling protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17556.11

構造登録者

Komander, D.,Odenwaelder, P.,Barford, D. (登録日: 2007-01-26, 公開日: 2008-02-05, 最終更新日: 2023-12-13)

主引用文献

Komander, D.,Reyes-Turcu, F.,Licchesi, J.D.F.,Odenwaelder, P.,Wilkinson, K.D.,Barford, D.
Molecular Discrimination of Structurally Equivalent Lys 63-Linked and Linear Polyubiquitin Chains.
Embo Rep., 10:466-, 2009

PubMed Abstract: At least eight types of ubiquitin chain exist, and individual linkages affect distinct cellular processes. The only distinguishing feature of differently linked ubiquitin chains is their structure, as polymers of the same unit are chemically identical. Here, we have crystallized Lys 63-linked and linear ubiquitin dimers, revealing that both adopt equivalent open conformations, forming no contacts between ubiquitin molecules and thereby differing significantly from Lys 48-linked ubiquitin chains. We also examined the specificity of various deubiquitinases (DUBs) and ubiquitin-binding domains (UBDs). All analysed DUBs, except CYLD, cleave linear chains less efficiently compared with other chain types, or not at all. Likewise, UBDs can show chain specificity, and are able to select distinct linkages from a ubiquitin chain mixture. We found that the UBAN (ubiquitin binding in ABIN and NEMO) motif of NEMO (NF-kappaB essential modifier) binds to linear chains exclusively, whereas the NZF (Npl4 zinc finger) domain of TAB2 (TAK1 binding protein 2) is Lys 63 specific. Our results highlight remarkable specificity determinants within the ubiquitin system.

PubMed: 19373254
DOI: 10.1038/EMBOR.2009.55

実験手法

X-RAY DIFFRACTION (1.95 Å)