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2W9N

crystal structure of linear di-ubiquitin

Summary for 2W9N
Entry DOI10.2210/pdb2w9n/pdb
Related1C3T 1D3Z 1F9J 1FXT 1G6J 1GJZ 1NBF 1OGW 1Q5W 1S1Q 1SIF 1TBE 1UBI 1UBQ 1XD3 1XQQ 1YX5 1YX6 1ZGU 2AYO 2BGF 2G45 2GBJ 2GBK 2GBM 2GBN 2J7Q 2JF5
DescriptorUBIQUITIN, ZINC ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordscell cycle, k63, ikk, nemo, lys63, linear, ubiquitin, signalling cell cycle
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains1
Total formula weight17460.75
Authors
Komander, D.,Reyes-Turcu, F.,Wilkinson, K.D.,Barford, D. (deposition date: 2009-01-27, release date: 2009-04-28, Last modification date: 2024-11-13)
Primary citationKomander, D.,Reyes-Turcu, F.,Licchesi, J.D.,Odenwaelder, P.,Wilkinson, K.D.,Barford, D.
Molecular Discrimination of Structurally Equivalent Lys 63-Linked and Linear Polyubiquitin Chains.
Embo Rep., 10:466-, 2009
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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