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PDBsum entry 3utm
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Transferase/signaling protein
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PDB id
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3utm
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PDB id:
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Transferase/signaling protein
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Title:
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Crystal structure of a mouse tankyrase-axin complex
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Structure:
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Tankyrase-1. Chain: a, b. Fragment: mtnks1 arc23 (unp residues 308-655). Synonym: tank1, trf1-interacting ankyrin-related adp-ribose polymerase 1, tankyrase i. Engineered: yes. Axin-1. Chain: c. Fragment: maxin1 n domain (unp residues 1-80).
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: tankryase1, tnks, tnks1. Expressed in: escherichia coli. Expression_system_taxid: 511693. Gene: axin, axin1, fu.
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Resolution:
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2.00Å
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R-factor:
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0.209
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R-free:
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0.238
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Authors:
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Z.Cheng,S.Morrone,W.Xu
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Key ref:
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S.Morrone
et al.
(2012).
Crystal structure of a Tankyrase-Axin complex and its implications for Axin turnover and Tankyrase substrate recruitment.
Proc Natl Acad Sci U S A,
109,
1500-1505.
PubMed id:
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Date:
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26-Nov-11
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Release date:
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18-Jan-12
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PROCHECK
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Headers
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References
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Enzyme class 1:
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Chains A, B:
E.C.2.4.2.-
- ?????
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Enzyme class 2:
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Chains A, B:
E.C.2.4.2.30
- NAD(+) ADP-ribosyltransferase.
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Pathway:
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Reaction:
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NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D- ribosyl)n+1-acceptor + H+
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NAD(+)
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+
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(ADP-D-ribosyl)n-acceptor
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=
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nicotinamide
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+
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(ADP-D- ribosyl)n+1-acceptor
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Proc Natl Acad Sci U S A
109:1500-1505
(2012)
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PubMed id:
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Crystal structure of a Tankyrase-Axin complex and its implications for Axin turnover and Tankyrase substrate recruitment.
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S.Morrone,
Z.Cheng,
R.T.Moon,
F.Cong,
W.Xu.
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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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J.L.Riffell,
C.J.Lord,
and
A.Ashworth
(2012).
Tankyrase-targeted therapeutics: expanding opportunities in the PARP family.
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Nat Rev Drug Discov,
11,
923-936.
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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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