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PDBsum entry 3jsv
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Signaling protein/transcription
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PDB id
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3jsv
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Contents |
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* Residue conservation analysis
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PDB id:
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Signaling protein/transcription
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Title:
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Crystal structure of mouse nemo cozi in complex with lys63-linked di- ubiquitin
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Structure:
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Ubiquitin. Chain: a. Engineered: yes. Mutation: yes. Ubiquitin. Chain: b. Engineered: yes. Mutation: yes. Nf-kappa-b essential modulator.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090. Gene: ikbkg, nemo, nemo(249-343).
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Resolution:
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2.70Å
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R-factor:
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0.250
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R-free:
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0.294
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Authors:
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A.Yoshikawa,Y.Sato,H.Mimura,M.Yamashita,A.Yamagata,S.Fukai
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Key ref:
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A.Yoshikawa
et al.
(2009).
Crystal structure of the NEMO ubiquitin-binding domain in complex with Lys 63-linked di-ubiquitin.
Febs Lett,
583,
3317-3322.
PubMed id:
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Date:
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11-Sep-09
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Release date:
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27-Oct-09
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PROCHECK
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Headers
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References
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P0CG48
(UBC_HUMAN) -
Polyubiquitin-C from Homo sapiens
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Seq: Struc:
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685 a.a.
76 a.a.*
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Febs Lett
583:3317-3322
(2009)
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PubMed id:
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Crystal structure of the NEMO ubiquitin-binding domain in complex with Lys 63-linked di-ubiquitin.
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A.Yoshikawa,
Y.Sato,
M.Yamashita,
H.Mimura,
A.Yamagata,
S.Fukai.
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ABSTRACT
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NEMO is essential for activation of the NF-kappaB signaling pathway, which is
regulated by ubiquitination of proteins. The C-terminal leucine zipper of NEMO
and its adjacent coiled-coil region (CC2-LZ) reportedly bind to linear ubiquitin
chains with 1 microM affinity and to Lys 63-linked chains with 100 microM
affinity. Here we report the crystal structure of the CC2-LZ region of mouse
NEMO in complex with Lys 63-linked di-ubiquitin (K63-Ub(2)) at 2.7A resolution.
The ubiquitin-binding region consists of a 130A-long helix and forms a parallel
coiled-coil dimer. The Ile 44-centered hydrophobic patch of ubiquitin is
recognized in the middle of the NEMO ubiquitin-binding region. NEMO interacts
with each K63-Ub(2)via a single ubiquitin-binding site, consistent with low
affinity binding with K63-Ub(2).
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.Kulathu,
and
D.Komander
(2012).
Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages.
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Nat Rev Mol Cell Biol,
13,
508-523.
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C.Behrends,
and
J.W.Harper
(2011).
Constructing and decoding unconventional ubiquitin chains.
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Nat Struct Mol Biol,
18,
520-528.
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C.Zheng,
Q.Yin,
and
H.Wu
(2011).
Structural studies of NF-κB signaling.
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Cell Res,
21,
183-195.
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S.Miyamoto
(2011).
Nuclear initiated NF-κB signaling: NEMO and ATM take center stage.
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Cell Res,
21,
116-130.
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F.Liu,
and
K.J.Walters
(2010).
Multitasking with ubiquitin through multivalent interactions.
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Trends Biochem Sci,
35,
352-360.
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H.Wu,
Y.C.Lo,
and
S.C.Lin
(2010).
Recent advances in polyubiquitin chain recognition.
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F1000 Biol Rep,
2,
1-5.
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J.Gautheron,
and
G.Courtois
(2010).
"Without Ub I am nothing": NEMO as a multifunctional player in ubiquitin-mediated control of NF-kappaB activation.
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Cell Mol Life Sci,
67,
3101-3113.
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Y.Kulathu,
M.Akutsu,
A.Bremm,
K.Hofmann,
and
D.Komander
(2009).
Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain.
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Nat Struct Mol Biol,
16,
1328-1330.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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