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PDBsum entry 3twv

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protein ligands Protein-protein interface(s) links
Signaling protein/peptide PDB id
3twv

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
155 a.a.
12 a.a.
11 a.a.
13 a.a.
Ligands
PE8 ×3
SO4 ×7
EDO ×6
Waters ×158
PDB id:
3twv
Name: Signaling protein/peptide
Title: Crystal structure of arc4 from human tankyrase 2 in complex with peptide from human numa1 (chimeric peptide)
Structure: Tankyrase-2. Chain: a, b, c, d. Fragment: unp residues 488-649. Synonym: tank2, poly [adp-ribose] polymerase 5b, tnks-2, trf1- interacting ankyrin-related adp-ribose polymerase 2, tankyrase ii, tankyrase-like protein, tankyrase-related protein. Engineered: yes. Human numa1. Chain: e, f, g, h.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: parp5b, tank2, tnkl, tnks2. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: solid-state synthesized peptide
Resolution:
2.30Å     R-factor:   0.190     R-free:   0.245
Authors: S.Guettler,F.Sicheri
Key ref: S.Guettler et al. (2011). Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease. Cell, 147, 1340-1354. PubMed id: 22153077
Date:
22-Sep-11     Release date:   07-Dec-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9H2K2  (TNKS2_HUMAN) -  Poly [ADP-ribose] polymerase tankyrase-2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1166 a.a.
155 a.a.
Protein chain
No UniProt id for this chain
Struc: 12 a.a.
Protein chains
No UniProt id for this chain
Struc: 11 a.a.
Protein chain
No UniProt id for this chain
Struc: 13 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: Chains A, B, C, D: E.C.2.4.2.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chains A, B, C, D: E.C.2.4.2.30  - NAD(+) ADP-ribosyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
      Reaction: NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D- ribosyl)n+1-acceptor + H+
NAD(+)
+ (ADP-D-ribosyl)n-acceptor
= nicotinamide
+ (ADP-D- ribosyl)n+1-acceptor
+ H(+)
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.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Cell 147:1340-1354 (2011)
PubMed id: 22153077  
 
 
Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease.
S.Guettler, J.LaRose, E.Petsalaki, G.Gish, A.Scotter, T.Pawson, R.Rottapel, F.Sicheri.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22713970 B.A.Gibson, and W.L.Kraus (2012).
New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs.
  Nat Rev Mol Cell Biol, 13, 411-424.  
23197039 J.L.Riffell, C.J.Lord, and A.Ashworth (2012).
Tankyrase-targeted therapeutics: expanding opportunities in the PARP family.
  Nat Rev Drug Discov, 11, 923-936.  
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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