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PDBsum entry 2x5n
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Nuclear protein
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PDB id
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2x5n
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Contents |
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* Residue conservation analysis
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PDB id:
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Nuclear protein
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Title:
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Crystal structure of the sprpn10 vwa domain
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Structure:
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26s proteasome regulatory subunit rpn10. Chain: a. Fragment: vwa domain, residues 2-193. Synonym: sprpn10. Engineered: yes
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Source:
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Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.30Å
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R-factor:
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0.125
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R-free:
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0.165
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Authors:
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C.Riedinger,J.Boehringer,J.-F.Trempe,E.D.Lowe,N.R.Brown,K.Gehring, M.E.M.Noble,C.Gordon,J.A.Endicott
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Key ref:
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C.Riedinger
et al.
(2010).
Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12.
J Biol Chem,
285,
33992-34003.
PubMed id:
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Date:
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10-Feb-10
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Release date:
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25-Aug-10
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PROCHECK
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Headers
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References
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O94444
(RPN10_SCHPO) -
26S proteasome regulatory subunit rpn10 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)
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Seq: Struc:
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243 a.a.
189 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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J Biol Chem
285:33992-34003
(2010)
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PubMed id:
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Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12.
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C.Riedinger,
J.Boehringer,
J.F.Trempe,
E.D.Lowe,
N.R.Brown,
K.Gehring,
M.E.Noble,
C.Gordon,
J.A.Endicott.
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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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G.C.Lander,
E.Estrin,
M.E.Matyskiela,
C.Bashore,
E.Nogales,
and
A.Martin
(2012).
Complete subunit architecture of the proteasome regulatory particle.
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Nature,
482,
186-191.
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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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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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');
}
}
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