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PDBsum entry 2c2l
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Contents |
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* Residue conservation analysis
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PDB id:
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Chaperone
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Title:
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Crystal structure of the chip u-box e3 ubiquitin ligase
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Structure:
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Carboxy terminus of hsp70-interacting protein. Chain: a, b, c, d. Synonym: chip. Engineered: yes. Hsp90. Chain: e, f, g, h. Fragment: c-terminal peptide, unp residues 414-422. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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3.30Å
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R-factor:
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0.248
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R-free:
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0.286
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Authors:
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M.Zhang,S.M.Roe,L.H.Pearl
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Key ref:
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M.Zhang
et al.
(2005).
Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.
Mol Cell,
20,
525-538.
PubMed id:
DOI:
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Date:
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29-Sep-05
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Release date:
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23-Nov-05
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PROCHECK
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Headers
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References
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Q9WUD1
(CHIP_MOUSE) -
E3 ubiquitin-protein ligase CHIP from Mus musculus
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Seq:
Struc:
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304 a.a.
281 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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DOI no:
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Mol Cell
20:525-538
(2005)
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PubMed id:
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Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.
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M.Zhang,
M.Windheim,
S.M.Roe,
M.Peggie,
P.Cohen,
C.Prodromou,
L.H.Pearl.
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ABSTRACT
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CHIP is a dimeric U box E3 ubiquitin ligase that binds Hsp90 and/or Hsp70 via
its TPR-domain, facilitating ubiquitylation of chaperone bound client proteins.
We have determined the crystal structure of CHIP bound to an Hsp90 C-terminal
decapeptide. The structure explains how CHIP associates with either chaperone
type and reveals an unusual asymmetric homodimer in which the protomers adopt
radically different conformations. Additionally, we identified CHIP as a
functional partner of Ubc13-Uev1a in formation of Lys63-linked polyubiquitin
chains, extending CHIP's roles into ubiquitin regulation as well as targeted
destruction. The structure of Ubc13-Uev1a bound to the CHIP U box domain defines
the basis for selective cooperation of CHIP with specific ubiquitin-conjugating
enzymes. Remarkably, the asymmetric arrangement of the TPR domains in the CHIP
dimer occludes one Ubc binding site, so that CHIP operates with half-of-sites
activity, providing an elegant means for coupling a dimeric chaperone to a
single ubiquitylation system.
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Selected figure(s)
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Figure 2.
Figure 2. Architecture of the CHIP Homodimer
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Figure 3.
Figure 3. Asymmetric Disposition of TPR Domains
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
20,
525-538)
copyright 2005.
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Figures were
selected
by an automated process.
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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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A.Plechanovová,
E.G.Jaffray,
M.H.Tatham,
J.H.Naismith,
and
R.T.Hay
(2012).
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.
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Nature,
489,
115-120.
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PDB code:
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H.Dou,
L.Buetow,
A.Hock,
G.J.Sibbet,
K.H.Vousden,
and
D.T.Huang
(2012).
Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl.
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Nat Struct Mol Biol,
19,
184-192.
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PDB codes:
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A.Plechanovová,
E.G.Jaffray,
S.A.McMahon,
K.A.Johnson,
I.Navrátilová,
J.H.Naismith,
and
R.T.Hay
(2011).
Mechanism of ubiquitylation by dimeric RING ligase RNF4.
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Nat Struct Mol Biol,
18,
1052-1059.
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PDB code:
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A.Salminen,
J.Ojala,
K.Kaarniranta,
M.Hiltunen,
and
H.Soininen
(2011).
Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease.
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Prog Neurobiol,
93,
99.
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G.E.Karagöz,
A.M.Duarte,
H.Ippel,
C.Uetrecht,
T.Sinnige,
M.van Rosmalen,
J.Hausmann,
A.J.Heck,
R.Boelens,
and
S.G.Rüdiger
(2011).
N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.
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Proc Natl Acad Sci U S A,
108,
580-585.
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H.Smith,
X.Y.Liu,
L.Dai,
E.T.Goh,
A.T.Chan,
J.Xi,
C.C.Seh,
I.A.Qureshi,
J.Lescar,
C.Ruedl,
R.Gourlay,
S.Morton,
J.Hough,
E.G.McIver,
P.Cohen,
and
P.C.Cheung
(2011).
The role of TBK1 and IKKϵ in the expression and activation of Pellino 1.
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Biochem J,
434,
537-548.
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Y.Zhang,
X.Zhou,
L.Zhao,
C.Li,
H.Zhu,
L.Xu,
L.Shan,
X.Liao,
Z.Guo,
and
P.Huang
(2011).
UBE2W interacts with FANCL and regulates the monoubiquitination of fanconi anemia protein FANCD2.
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Mol Cells,
31,
113-122.
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A.R.Cole,
L.P.Lewis,
and
H.Walden
(2010).
The structure of the catalytic subunit FANCL of the Fanconi anemia core complex.
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Nat Struct Mol Biol,
17,
294-298.
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PDB code:
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D.M.Wenzel,
K.E.Stoll,
and
R.E.Klevit
(2010).
E2s: structurally economical and functionally replete.
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Biochem J,
433,
31-42.
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H.H.Kampinga,
and
E.A.Craig
(2010).
The HSP70 chaperone machinery: J proteins as drivers of functional specificity.
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Nat Rev Mol Cell Biol,
11,
579-592.
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J.Tao,
K.Petrova,
D.Ron,
and
B.Sha
(2010).
Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR.
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J Mol Biol,
397,
1307-1315.
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PDB code:
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K.A.Nordquist,
Y.N.Dimitrova,
P.S.Brzovic,
W.B.Ridenour,
K.A.Munro,
S.E.Soss,
R.M.Caprioli,
R.E.Klevit,
and
W.J.Chazin
(2010).
Structural and functional characterization of the monomeric U-box domain from E4B.
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Biochemistry,
49,
347-355.
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PDB code:
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L.Kundrat,
and
L.Regan
(2010).
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP.
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J Mol Biol,
395,
587-594.
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P.D.Mace,
S.Shirley,
and
C.L.Day
(2010).
Assembling the building blocks: structure and function of inhibitor of apoptosis proteins.
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Cell Death Differ,
17,
46-53.
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Q.Huang,
and
M.E.Figueiredo-Pereira
(2010).
Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implications.
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Apoptosis,
15,
1292-1311.
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R.C.Benirschke,
J.R.Thompson,
Y.Nominé,
E.Wasielewski,
N.JuraniÄ,
S.Macura,
S.Hatakeyama,
K.I.Nakayama,
M.V.Botuyan,
and
G.Mer
(2010).
Molecular basis for the association of human E4B U box ubiquitin ligase with E2-conjugating enzymes UbcH5c and Ubc4.
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Structure,
18,
955-965.
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PDB codes:
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S.Matsunaga,
K.Matsuoka,
K.Shimizu,
Y.Endo,
and
T.Sawasaki
(2010).
Biotinylated-sortase self-cleavage purification (BISOP) method for cell-free produced proteins.
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BMC Biotechnol,
10,
42.
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S.Yan,
X.Sun,
B.Xiang,
H.Cang,
X.Kang,
Y.Chen,
H.Li,
G.Shi,
E.T.Yeh,
B.Wang,
X.Wang,
and
J.Yi
(2010).
Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90.
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EMBO J,
29,
3773-3786.
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T.Maruyama,
H.Kadowaki,
N.Okamoto,
A.Nagai,
I.Naguro,
A.Matsuzawa,
H.Shibuya,
K.Tanaka,
S.Murata,
K.Takeda,
H.Nishitoh,
and
H.Ichijo
(2010).
CHIP-dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic response.
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EMBO J,
29,
2501-2514.
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T.Okiyoneda,
H.Barrière,
M.Bagdány,
W.M.Rabeh,
K.Du,
J.Höhfeld,
J.C.Young,
and
G.L.Lukacs
(2010).
Peripheral protein quality control removes unfolded CFTR from the plasma membrane.
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Science,
329,
805-810.
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T.P.Yao
(2010).
The role of ubiquitin in autophagy-dependent protein aggregate processing.
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Genes Cancer,
1,
779-786.
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A.A.Yunus,
and
C.D.Lima
(2009).
Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.
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Mol Cell,
35,
669-682.
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PDB code:
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D.E.Christensen,
and
R.E.Klevit
(2009).
Dynamic interactions of proteins in complex networks: identifying the complete set of interacting E2s for functional investigation of E3-dependent protein ubiquitination.
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FEBS J,
276,
5381-5389.
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G.Liu,
F.Forouhar,
A.Eletsky,
H.S.Atreya,
J.M.Aramini,
R.Xiao,
Y.J.Huang,
M.Abashidze,
J.Seetharaman,
J.Liu,
B.Rost,
T.Acton,
G.T.Montelione,
J.F.Hunt,
and
T.Szyperski
(2009).
NMR and X-RAY structures of human E2-like ubiquitin-fold modifier conjugating enzyme 1 (UFC1) reveal structural and functional conservation in the metazoan UFM1-UBA5-UFC1 ubiquination pathway.
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J Struct Funct Genomics,
10,
127-136.
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PDB codes:
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H.Smith,
M.Peggie,
D.G.Campbell,
F.Vandermoere,
E.Carrick,
and
P.Cohen
(2009).
Identification of the phosphorylation sites on the E3 ubiquitin ligase Pellino that are critical for activation by IRAK1 and IRAK4.
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Proc Natl Acad Sci U S A,
106,
4584-4590.
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J.A.Marteijn,
L.T.van der Meer,
J.J.Smit,
S.M.Noordermeer,
W.Wissink,
P.Jansen,
H.G.Swarts,
R.G.Hibbert,
T.de Witte,
T.K.Sixma,
J.H.Jansen,
and
B.A.van der Reijden
(2009).
The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains.
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Leukemia,
23,
1480-1489.
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J.Li,
X.Qian,
J.Hu,
and
B.Sha
(2009).
Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading.
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J Biol Chem,
284,
23852-23859.
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PDB codes:
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N.Zhang,
R.Kaur,
S.Akhter,
and
R.J.Legerski
(2009).
Cdc5L interacts with ATR and is required for the S-phase cell-cycle checkpoint.
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EMBO Rep,
10,
1029-1035.
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Q.Yin,
S.C.Lin,
B.Lamothe,
M.Lu,
Y.C.Lo,
G.Hura,
L.Zheng,
R.L.Rich,
A.D.Campos,
D.G.Myszka,
M.J.Lenardo,
B.G.Darnay,
and
H.Wu
(2009).
E2 interaction and dimerization in the crystal structure of TRAF6.
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Nat Struct Mol Biol,
16,
658-666.
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PDB codes:
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R.J.Deshaies,
and
C.A.Joazeiro
(2009).
RING domain E3 ubiquitin ligases.
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Annu Rev Biochem,
78,
399-434.
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S.B.Qian,
L.Waldron,
N.Choudhary,
R.E.Klevit,
W.J.Chazin,
and
C.Patterson
(2009).
Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transfer.
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J Biol Chem,
284,
26797-26802.
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X.Ding,
and
M.S.Goldberg
(2009).
Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP.
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PLoS One,
4,
e5949.
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X.Duan,
P.Sarangi,
X.Liu,
G.K.Rangi,
X.Zhao,
and
H.Ye
(2009).
Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex.
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Mol Cell,
35,
657-668.
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PDB code:
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Y.Ye,
and
M.Rape
(2009).
Building ubiquitin chains: E2 enzymes at work.
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Nat Rev Mol Cell Biol,
10,
755-764.
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B.J.Winborn,
S.M.Travis,
S.V.Todi,
K.M.Scaglione,
P.Xu,
A.J.Williams,
R.E.Cohen,
J.Peng,
and
H.L.Paulson
(2008).
The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains.
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J Biol Chem,
283,
26436-26443.
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C.R.Langelier,
V.Sandrin,
D.M.Eckert,
D.E.Christensen,
V.Chandrasekaran,
S.L.Alam,
C.Aiken,
J.C.Olsen,
A.K.Kar,
J.G.Sodroski,
and
W.I.Sundquist
(2008).
Biochemical characterization of a recombinant TRIM5alpha protein that restricts human immunodeficiency virus type 1 replication.
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J Virol,
82,
11682-11694.
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D.Han,
K.Kim,
J.Oh,
J.Park,
and
Y.Kim
(2008).
TPR domain of NrfG mediates complex formation between heme lyase and formate-dependent nitrite reductase in Escherichia coli O157:H7.
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Proteins,
70,
900-914.
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PDB code:
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D.T.Huang,
M.Zhuang,
O.Ayrault,
and
B.A.Schulman
(2008).
Identification of conjugation specificity determinants unmasks vestigial preference for ubiquitin within the NEDD8 E2.
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Nat Struct Mol Biol,
15,
280-287.
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J.L.Parsons,
P.S.Tait,
D.Finch,
I.I.Dianova,
S.L.Allinson,
and
G.L.Dianov
(2008).
CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins.
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Mol Cell,
29,
477-487.
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K.Linke,
P.D.Mace,
C.A.Smith,
D.L.Vaux,
J.Silke,
and
C.L.Day
(2008).
Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans.
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Cell Death Differ,
15,
841-848.
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PDB codes:
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M.Minakawa,
T.Sone,
T.Takeuchi,
and
H.Yokosawa
(2008).
Regulation of the nuclear factor (NF)-kappaB pathway by ISGylation.
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| |
Biol Pharm Bull,
31,
2223-2227.
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M.Palaiomylitou,
A.Tartas,
D.Vlachakis,
D.Tzamarias,
and
M.Vlassi
(2008).
Investigating the structural stability of the Tup1-interaction domain of Ssn6: evidence for a conformational change on the complex.
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Proteins,
70,
72-82.
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M.S.Huen,
J.Huang,
J.Yuan,
M.Yamamoto,
S.Akira,
C.Ashley,
W.Xiao,
and
J.Chen
(2008).
Noncanonical E2 variant-independent function of UBC13 in promoting checkpoint protein assembly.
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Mol Cell Biol,
28,
6104-6112.
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M.Zhang,
M.Botër,
K.Li,
Y.Kadota,
B.Panaretou,
C.Prodromou,
K.Shirasu,
and
L.H.Pearl
(2008).
Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes.
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EMBO J,
27,
2789-2798.
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PDB code:
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N.Ponts,
J.Yang,
D.W.Chung,
J.Prudhomme,
T.Girke,
P.Horrocks,
and
K.G.Le Roch
(2008).
Deciphering the ubiquitin-mediated pathway in apicomplexan parasites: a potential strategy to interfere with parasite virulence.
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| |
PLoS ONE,
3,
e2386.
|
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P.D.Mace,
K.Linke,
R.Feltham,
F.R.Schumacher,
C.A.Smith,
D.L.Vaux,
J.Silke,
and
C.L.Day
(2008).
Structures of the cIAP2 RING Domain Reveal Conformational Changes Associated with Ubiquitin-conjugating Enzyme (E2) Recruitment.
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| |
J Biol Chem,
283,
31633-31640.
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PDB codes:
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S.H.Millson,
C.K.Vaughan,
C.Zhai,
M.M.Ali,
B.Panaretou,
P.W.Piper,
L.H.Pearl,
and
C.Prodromou
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PDB code:
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J Mol Biol,
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PDB code:
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Proc Natl Acad Sci U S A,
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PDB codes:
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Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages.
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J Biol Chem,
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PDB code:
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PDB code:
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I.Al-Ramahi,
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PDB code:
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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
code is
shown on the right.
|
|
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