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PDBsum entry 2jsd

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protein ligands metals links
Hydrolase PDB id
2jsd
Jmol
Contents
Protein chain
160 a.a. *
Ligands
NGH
Metals
_CA ×2
_ZN ×2
* Residue conservation analysis
PDB id:
2jsd
Name: Hydrolase
Title: Solution structure of mmp20 complexed with nngh
Structure: Matrix metalloproteinase-20. Chain: a. Fragment: catalytic domain, residues 113-272. Synonym: mmp-20, enamel metalloproteinase, enamelysin. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: odontoblast. Gene: mmp20. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 20 models
Authors: Y.Arendt,L.Banci,I.Bertini,F.Cantini,R.Cozzi,R.Del Conte, L.Gonnelli,Structural Proteomics In Europe (Spine)
Key ref: Y.Arendt et al. (2007). Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase. FEBS Lett, 581, 4723-4726. PubMed id: 17869250 DOI: 10.1016/j.febslet.2007.08.069
Date:
03-Jul-07     Release date:   20-Nov-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O60882  (MMP20_HUMAN) -  Matrix metalloproteinase-20
Seq:
Struc:
483 a.a.
160 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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: 10.1016/j.febslet.2007.08.069 FEBS Lett 581:4723-4726 (2007)
PubMed id: 17869250  
 
 
Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.
Y.Arendt, L.Banci, I.Bertini, F.Cantini, R.Cozzi, R.Del Conte, L.Gonnelli.
 
  ABSTRACT  
 
The solution structure of the catalytic domain of MMP-20, a member of the matrix metalloproteinases family not yet structurally characterized, complexed with N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH), is here reported and compared with other MMPs-NNGH adducts. The backbone dynamic has been characterized as well. We have found that, despite the same fold and very high overall similarity, the present structure experiences specific structural and dynamical similarities with some MMPs and differences with others, around the catalytic cavity. The present solution structure, not only contributes to fill the gap of structural knowledge on human MMPs, but also provides further information to design more selective and efficient inhibitors for a specific member of this class of proteins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19126645 V.Nikolova, C.Y.Koo, S.A.Ibrahim, Z.Wang, D.Spillmann, R.Dreier, R.Kelsch, J.Fischgräbe, M.Smollich, L.H.Rossi, W.Sibrowski, P.Wülfing, L.Kiesel, G.W.Yip, and M.Götte (2009).
Differential roles for membrane-bound and soluble syndecan-1 (CD138) in breast cancer progression.
  Carcinogenesis, 30, 397-407.  
18629001 T.Pauly, M.Ratliff, E.Pietrowski, R.Neugebauer, A.Schlicksupp, J.Kirsch, and J.Kuhse (2008).
Activity-dependent shedding of the NMDA receptor glycine binding site by matrix metalloproteinase 3: a PUTATIVE mechanism of postsynaptic plasticity.
  PLoS ONE, 3, e2681.  
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