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PDBsum entry 2bua
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protein ligands Protein-protein interface(s) links
Hydrolase/inhibitor PDB id
2bua

 

 

 

 

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Contents
Protein chains
728 a.a. *
Ligands
NAG-NAG ×9
NAG ×15
007 ×4
SO4 ×8
Waters ×826
* Residue conservation analysis
PDB id:
2bua
Name: Hydrolase/inhibitor
Title: Crystal structure of porcine dipeptidyl peptidase iv (cd26) in complex with a low molecular weight inhibitor.
Structure: Dipeptidyl peptidase iv. Chain: a, b, c, d. Fragment: extracellular domain, residues 39-766. Synonym: dpp iv, t-cell activation antigen cd26. Ec: 3.4.14.5
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organ: kidney cortex
Biol. unit: Dimer (from PDB file)
Resolution:
2.56Å     R-factor:   0.220     R-free:   0.256
Authors: S.Nordhoff,S.Cerezo-Galvez,A.Feurer,O.Hill,V.G.Matassa,G.Metz, C.Rummey,M.Thiemann,P.J.Edwards
Key ref: S.Nordhoff et al. (2006). The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors. Bioorg Med Chem Lett, 16, 1744-1748. PubMed id: 16376544 DOI: 10.1016/j.bmcl.2005.11.103
Date:
09-Jun-05     Release date:   23-Jan-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P22411  (DPP4_PIG) -  Dipeptidyl peptidase 4 from Sus scrofa
Seq:
Struc: 		 
Seq:
Struc: 		766 a.a.
728 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.14.5  - dipeptidyl-peptidase Iv.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Release of an N-terminal dipeptide, Xaa-Xbb-|-Xcc, from a polypeptide, preferentially when Xbb is Pro, provided Xcc is neither Pro nor hydroxyproline.

 

 
DOI no: 10.1016/j.bmcl.2005.11.103 Bioorg Med Chem Lett 16:1744-1748 (2006)
PubMed id: 16376544  
 
 
The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors.
S.Nordhoff, S.Cerezo-Gálvez, A.Feurer, O.Hill, V.G.Matassa, G.Metz, C.Rummey, M.Thiemann, P.J.Edwards.
 
  ABSTRACT  
 
The co-crystal structure of beta-phenethylamine fragment inhibitor 5 bound to DPP-IV revealed that the phenyl ring occupied the proline pocket of the enzyme. This finding provided the basis for a general hypothesis of a reverse binding mode for beta-phenethylamine-based DPP-IV inhibitors. Novel inhibitor design concepts that obviate substrate-like structure-activity relationships (SAR) were thereby enabled, and novel, potent inhibitors were discovered.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17068815 C.Rummey, and G.Metz (2007).
Homology models of dipeptidyl peptidases 8 and 9 with a focus on loop predictions near the active site.
  Proteins, 66, 160-171.  
17492130 H.Hiramatsu, K.Kyono, A.Yamamoto, K.Saeki, H.Shima, S.Sugiyama, K.Inaka, and R.Shimizu (2007).
Crystal structures of human dipeptidyl peptidase IV in its apo and diprotin B-complexed forms.
  Acta Biochim Biophys Sin (Shanghai), 39, 335-343.  
17618469 J.Zeng, G.Liu, Y.Tang, and H.Jiang (2007).
3D-QSAR studies on fluoropyrrolidine amides as dipeptidyl peptidase IV inhibitors by CoMFA and CoMSIA.
  J Mol Model, 13, 993.  
17676345 R.R.Pissurlenkar, M.S.Shaikh, and E.C.Coutinho (2007).
3D-QSAR studies of Dipeptidyl peptidase IV inhibitors using a docking based alignment.
  J Mol Model, 13, 1047-1071.  
17084612 D.A.Erlanson (2006).
Fragment-based lead discovery: a chemical update.
  Curr Opin Biotechnol, 17, 643-652.  
17112720 P.R.Mittl, and M.G.Grütter (2006).
Opportunities for structure-based design of protease-directed drugs.
  Curr Opin Struct Biol, 16, 769-775.  
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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