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PDBsum entry 3nob
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Protein binding
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PDB id
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3nob
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Protein binding
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Title:
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Structure of k11-linked di-ubiquitin
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Structure:
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Ubiquitin. Chain: a, b, c, d, e, f, g, h. Engineered: yes
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Source:
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Homo sapiens. Organism_taxid: 9606. Gene: rps27a, uba80, ubcep1, uba52, ubb, ubc. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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2.19Å
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R-factor:
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0.247
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R-free:
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0.281
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Authors:
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K.C.Dong,M.L.Matsumoto,S.G.Hymowitz
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Key ref:
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M.L.Matsumoto
et al.
(2010).
K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody.
Mol Cell,
39,
477-484.
PubMed id:
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Date:
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25-Jun-10
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Release date:
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11-Aug-10
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PROCHECK
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Headers
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References
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P62979
(RS27A_HUMAN) -
Ubiquitin-ribosomal protein eS31 fusion protein from Homo sapiens
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Seq:
Struc:
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156 a.a.
77 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Mol Cell
39:477-484
(2010)
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PubMed id:
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K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody.
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M.L.Matsumoto,
K.E.Wickliffe,
K.C.Dong,
C.Yu,
I.Bosanac,
D.Bustos,
L.Phu,
D.S.Kirkpatrick,
S.G.Hymowitz,
M.Rape,
R.F.Kelley,
V.M.Dixit.
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ABSTRACT
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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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L.Feng,
and
J.Chen
(2012).
The E3 ligase RNF8 regulates KU80 removal and NHEJ repair.
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Nat Struct Mol Biol,
19,
201-206.
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N.V.Dimova,
N.A.Hathaway,
B.H.Lee,
D.S.Kirkpatrick,
M.L.Berkowitz,
S.P.Gygi,
D.Finley,
and
R.W.King
(2012).
APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1.
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Nat Cell Biol,
14,
168-176.
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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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A.M.Weissman,
N.Shabek,
and
A.Ciechanover
(2011).
The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation.
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Nat Rev Mol Cell Biol,
12,
605-620.
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A.Saha,
S.Lewis,
G.Kleiger,
B.Kuhlman,
and
R.J.Deshaies
(2011).
Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate.
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Mol Cell,
42,
75-83.
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B.Gerlach,
S.M.Cordier,
A.C.Schmukle,
C.H.Emmerich,
E.Rieser,
T.L.Haas,
A.I.Webb,
J.A.Rickard,
H.Anderton,
W.W.Wong,
U.Nachbur,
L.Gangoda,
U.Warnken,
A.W.Purcell,
J.Silke,
and
H.Walczak
(2011).
Linear ubiquitination prevents inflammation and regulates immune signalling.
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Nature,
471,
591-596.
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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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E.W.Harhaj,
and
V.M.Dixit
(2011).
Deubiquitinases in the regulation of NF-κB signaling.
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Cell Res,
21,
22-39.
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J.R.McLean,
D.Chaix,
M.D.Ohi,
and
K.L.Gould
(2011).
State of the APC/C: organization, function, and structure.
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Crit Rev Biochem Mol Biol,
46,
118-136.
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K.E.Wickliffe,
S.Lorenz,
D.E.Wemmer,
J.Kuriyan,
and
M.Rape
(2011).
The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2.
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Cell,
144,
769-781.
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B.A.Malynn,
and
A.Ma
(2010).
Ubiquitin makes its mark on immune regulation.
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Immunity,
33,
843-852.
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F.Ikeda,
N.Crosetto,
and
I.Dikic
(2010).
What determines the specificity and outcomes of ubiquitin signaling?
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Cell,
143,
677-681.
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J.N.Dynek,
T.Goncharov,
E.C.Dueber,
A.V.Fedorova,
A.Izrael-Tomasevic,
L.Phu,
E.Helgason,
W.J.Fairbrother,
K.Deshayes,
D.S.Kirkpatrick,
and
D.Vucic
(2010).
c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling.
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EMBO J,
29,
4198-4209.
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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.
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Links
