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PDBsum entry 2jf5
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Signaling protein
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PDB id
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2jf5
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References listed in PDB file
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Key reference
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Title
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Molecular discrimination of structurally equivalent lys 63-Linked and linear polyubiquitin chains.
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Authors
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D.Komander,
F.Reyes-Turcu,
J.D.Licchesi,
P.Odenwaelder,
K.D.Wilkinson,
D.Barford.
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Ref.
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Embo Rep, 2009,
10,
466-473.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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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.
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