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PDBsum entry 2oy2
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Human mmp-8 in complex with peptide iag
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Structure:
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Neutrophil collagenase. Chain: a, f. Fragment: catalytic domain. Synonym: matrix metalloproteinase-8, mmp-8, pmnl collagenase, pmnl- cl. Engineered: yes. Ile-ala-gly peptide. Chain: w, y. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp8, clg1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes
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Resolution:
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1.50Å
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R-factor:
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0.166
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R-free:
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0.192
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Authors:
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V.Calderone,I.Bertini,M.Fragai,C.Luchinat,M.Maletta,K.J.Yeo
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Key ref:
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I.Bertini
et al.
(2006).
Snapshots of the reaction mechanism of matrix metalloproteinases.
Angew Chem Int Ed Engl,
45,
7952-7955.
PubMed id:
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Date:
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21-Feb-07
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Release date:
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06-Mar-07
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PROCHECK
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Headers
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References
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P22894
(MMP8_HUMAN) -
Neutrophil collagenase from Homo sapiens
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Seq:
Struc:
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467 a.a.
157 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.4.24.34
- neutrophil collagenase.
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Reaction:
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Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.
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Cofactor:
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Ca(2+); Zn(2+)
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Angew Chem Int Ed Engl
45:7952-7955
(2006)
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PubMed id:
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Snapshots of the reaction mechanism of matrix metalloproteinases.
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I.Bertini,
V.Calderone,
M.Fragai,
C.Luchinat,
M.Maletta,
K.J.Yeo.
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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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I.Bertini,
M.Fragai,
C.Luchinat,
M.Melikian,
and
C.Venturi
(2009).
Characterisation of the MMP-12-elastin adduct.
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Chemistry,
15,
7842-7845.
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I.Bertini,
M.Fragai,
C.Luchinat,
M.Melikian,
E.Mylonas,
N.Sarti,
and
D.I.Svergun
(2009).
Interdomain Flexibility in Full-length Matrix Metalloproteinase-1 (MMP-1).
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J Biol Chem,
284,
12821-12828.
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M.Rouffet,
C.Denhez,
E.Bourguet,
F.Bohr,
and
D.Guillaume
(2009).
In silico study of MMP inhibition.
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Org Biomol Chem,
7,
3817-3825.
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P.J.Baker,
K.L.Britton,
M.Fisher,
J.Esclapez,
C.Pire,
M.J.Bonete,
J.Ferrer,
and
D.W.Rice
(2009).
Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily.
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Proc Natl Acad Sci U S A,
106,
779-784.
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PDB codes:
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C.Andreini,
I.Bertini,
G.Cavallaro,
G.L.Holliday,
and
J.M.Thornton
(2008).
Metal ions in biological catalysis: from enzyme databases to general principles.
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J Biol Inorg Chem,
13,
1205-1218.
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I.Sagi,
and
M.E.Milla
(2008).
Application of structural dynamic approaches provide novel insights into the enzymatic mechanism of the tumor necrosis factor-alpha-converting enzyme.
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Anal Biochem,
372,
1.
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R.Bhaskaran,
M.O.Palmier,
J.L.Lauer-Fields,
G.B.Fields,
and
S.R.Van Doren
(2008).
MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.
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J Biol Chem,
283,
21779-21788.
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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.
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J Biol Inorg Chem,
12,
1197-1206.
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PDB codes:
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R.Bhaskaran,
M.O.Palmier,
N.A.Bagegni,
X.Liang,
and
S.R.Van Doren
(2007).
Solution structure of inhibitor-free human metalloelastase (MMP-12) indicates an internal conformational adjustment.
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J Mol Biol,
374,
1333-1344.
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PDB code:
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
