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Metalloprotease PDB id
1bqo
Jmol
Contents
Protein chains
169 a.a. *
Ligands
N25
Metals
_CA ×6
_ZN ×4
Waters ×75
* Residue conservation analysis
PDB id:
1bqo
Name: Metalloprotease
Title: Discovery of potent, achiral matrix metalloproteinase inhibi
Structure: Stromelysin-1. Chain: a, b. Synonym: mmp-3. Engineered: yes. Other_details: complexed to pg-117025
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.30Å     R-factor:   0.229     R-free:   0.294
Authors: S.Pikul,K.L.M.Dunham,N.G.Almstead,B.De,M.G.Natchus,M.V.Anast S.J.Mcphail,C.E.Snider,Y.O.Taiwo,T.J.Rydel,C.M.Dunaway,F.Gu G.E.Mieling
Key ref: S.Pikul et al. (1998). Discovery of potent, achiral matrix metalloproteinase inhibitors. J Med Chem, 41, 3568-3571. PubMed id: 9733482 DOI: 10.1021/jm980253r
Date:
17-Aug-98     Release date:   17-Aug-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08254  (MMP3_HUMAN) -  Stromelysin-1
Seq:
Struc:
477 a.a.
169 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.17  - Stromelysin 1.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
      Cofactor: Calcium; Zinc
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular matrix   1 term 
  Biological process     proteolysis   1 term 
  Biochemical function     metallopeptidase activity     3 terms  

 

 
DOI no: 10.1021/jm980253r J Med Chem 41:3568-3571 (1998)
PubMed id: 9733482  
 
 
Discovery of potent, achiral matrix metalloproteinase inhibitors.
S.Pikul, K.L.McDow Dunham, N.G.Almstead, B.De, M.G.Natchus, M.V.Anastasio, S.J.McPhail, C.E.Snider, Y.O.Taiwo, T.Rydel, C.M.Dunaway, F.Gu, G.E.Mieling.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20107670 D.Koda, T.Maruyama, N.Minakuchi, K.Nakashima, and M.Goto (2010).
Proteinase-mediated drastic morphological change of peptide-amphiphile to induce supramolecular hydrogelation.
  Chem Commun (Camb), 46, 979-981.  
19765281 M.M.Thwin, E.Douni, P.Arjunan, G.Kollias, P.V.Kumar, and P.Gopalakrishnakone (2009).
Suppressive effect of secretory phospholipase A2 inhibitory peptide on interleukin-1beta-induced matrix metalloproteinase production in rheumatoid synovial fibroblasts, and its antiarthritic activity in hTNFtg mice.
  Arthritis Res Ther, 11, R138.  
17699594 F.M.Tholozan, C.Gribbon, Z.Li, M.W.Goldberg, A.R.Prescott, N.McKie, and R.A.Quinlan (2007).
FGF-2 release from the lens capsule by MMP-2 maintains lens epithelial cell viability.
  Mol Biol Cell, 18, 4222-4231.  
17710450 L.A.Alcaraz, L.Banci, I.Bertini, F.Cantini, A.Donaire, and L.Gonnelli (2007).
Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.
  J Biol Inorg Chem, 12, 1197-1206.
PDB codes: 2jnp 2jt5 2jt6
16859524 N.Simard, G.Boire, A.J.de Brum-Fernandes, and Y.St-Pierre (2006).
A novel approach to measure the contribution of matrix metalloproteinase in the overall net proteolytic activity present in synovial fluids of patients with arthritis.
  Arthritis Res Ther, 8, R125.  
16261825 K.C.Sorensen, R.G.Newman, B.E.Kitchell, D.J.Schaeffer, and A.M.Siegel (2005).
Isolation, characterization, and expression of stromelysin-1 in primary tumors of dogs.
  Am J Vet Res, 66, 1526-1535.  
15254267 S.Kansra, S.W.Stoll, J.L.Johnson, and J.T.Elder (2004).
Autocrine extracellular signal-regulated kinase (ERK) activation in normal human keratinocytes: metalloproteinase-mediated release of amphiregulin triggers signaling from ErbB1 to ERK.
  Mol Biol Cell, 15, 4299-4309.  
14732707 V.Lukacova, Y.Zhang, M.Mackov, P.Baricic, S.Raha, J.A.Calvo, and S.Balaz (2004).
Similarity of binding sites of human matrix metalloproteinases.
  J Biol Chem, 279, 14194-14200.  
  12438450 J.Yang, R.W.Shultz, W.M.Mars, R.E.Wegner, Y.Li, C.Dai, K.Nejak, and Y.Liu (2002).
Disruption of tissue-type plasminogen activator gene in mice reduces renal interstitial fibrosis in obstructive nephropathy.
  J Clin Invest, 110, 1525-1538.  
12163483 M.Kaup, K.Dassler, C.Weise, and H.Fuchs (2002).
Shedding of the transferrin receptor is mediated constitutively by an integral membrane metalloprotease sensitive to tumor necrosis factor alpha protease inhibitor-2.
  J Biol Chem, 277, 38494-38502.  
10415719 B.De, M.G.Natchus, M.Cheng, S.Pikul, N.G.Almstead, Y.O.Taiwo, C.E.Snider, L.Chen, B.Barnett, F.Gu, and M.Dowty (1999).
The next generation of MMP inhibitors. Design and synthesis.
  Ann N Y Acad Sci, 878, 40-60.  
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 codes are shown on the right.