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PDBsum entry 1ck7
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* Residue conservation analysis
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Enzyme class:
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E.C.3.4.24.24
- gelatinase A.
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Reaction:
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Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
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Cofactor:
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Ca(2+); Zn(2+)
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DOI no:
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Science
284:1667-1670
(1999)
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PubMed id:
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Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
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E.Morgunova,
A.Tuuttila,
U.Bergmann,
M.Isupov,
Y.Lindqvist,
G.Schneider,
K.Tryggvason.
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ABSTRACT
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Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation.
Control of their activity is a promising target for therapy of diseases
characterized by abnormal connective tissue turnover. MMPs are expressed as
latent proenzymes that are activated by proteolytic cleavage that triggers a
conformational change in the propeptide (cysteine switch). The structure of
proMMP-2 reveals how the propeptide shields the catalytic cleft and that the
cysteine switch may operate through cleavage of loops essential for propeptide
stability.
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Selected figure(s)
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Figure 1.
Fig. 1. Structure of proMMP-2. The prodomain, catalytic domain,
fibronectin domains, and hemopexin domain are shown in red,
blue, green, and yellow, respectively. Zn^2+ ions are indicated
in red, and Ca^2+ ions are magenta (24). Asterisk indicates the
cleavage site for MT1-MMP.
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Figure 3.
Fig. 3. Structure of fibronectin domains (24). (A) Stereoview
of the electron density map contoured around cis-Pro^236 (P236)
and the Cys^233 (C233) to Cys^259 (C259) disulfide bridge.
Sulfur atoms are yellow. (B) Ribbon representation showing the
secondary structure with the disulfide bridges. (C and D)
Molecular surface of the fibronectin domains show polar (green)
and hydrophobic (red) residues that bind to gelatin (19). The
orientation in (B) and (C) is the same, and the molecule in (D)
is rotated by 180°. F, Phe; L, Leu; W, Trp.
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Figure 4.
Fig. 4. Interaction between propeptide and fibronectin
domains (24). (A) Stereoview of the propeptide residues in
contact with the hydrophobic pocket of the third fibronectin
domain. Hydrophobic residues from the fibronectin domain are
magenta and propeptide residues are yellow. Arg^368 (R368) and
Gly^367 (G367) (cyan) form hydrogen bonds with the propeptide
residues Asp^40 (D40) and Ile^35 (I35), respectively. (B)
Molecular surface of full-length proMMP-2. Colored surfaces
associated are with negatively charged (red) and positively
charged (blue) residues. Propeptide residues are represented as
a ball-and-stick model. Y, Tyr.
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The above figures are
reprinted
by permission from the AAAs:
Science
(1999,
284,
1667-1670)
copyright 1999.
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Figures were
selected
by an automated process.
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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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G.Murphy,
and
H.Nagase
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FEBS J,
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M.Ruehl,
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and
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Hydroxyproline-containing collagen analogs trigger the release and activation of collagen-sequestered proMMP-2 by competition with prodomain-derived peptide P33-42.
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Fibrogenesis Tissue Repair,
4,
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A.D.Kandasamy,
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A.Mauro,
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P.Tao,
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PLoS One,
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Biochem Biophys Res Commun,
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B.Tuysuz,
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and
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A novel matrix metalloproteinase 2 (MMP2) terminal hemopexin domain mutation in a family with multicentric osteolysis with nodulosis and arthritis with cardiac defects.
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Eur J Hum Genet,
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J Biol Chem,
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Enzymatic processing of beta-dystroglycan recombinant ectodomain by MMP-9: identification of the main cleavage site.
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IUBMB Life,
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O.A.Ozhogina,
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Characterization of the kringle fold and identification of a ubiquitous new class of disulfide rotamers.
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J Struct Biol,
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O.Veiseh,
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Small,
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P.Tao,
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Matrix metalloproteinase 2 inhibition: combined quantum mechanics and molecular mechanics studies of the inhibition mechanism of (4-phenoxyphenylsulfonyl)methylthiirane and its oxirane analogue.
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Biochemistry,
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Biochemistry,
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G.Murphy,
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Mol Aspects Med,
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Peptides,
29,
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M.Yamada,
Y.Sankoda,
R.Tatsumi,
W.Mizunoya,
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and
R.E.Allen
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Matrix metalloproteinase-2 mediates stretch-induced activation of skeletal muscle satellite cells in a nitric oxide-dependent manner.
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Int J Biochem Cell Biol,
40,
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N.Díaz,
and
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Proteins,
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W.J.Habraken,
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A.B.Hamze,
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and
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Protein Sci,
16,
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A.K.Chow,
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and
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Br J Pharmacol,
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A.Zankl,
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and
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(2007).
Torg syndrome is caused by inactivating mutations in MMP2 and is allelic to NAO and Winchester syndrome.
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J Bone Miner Res,
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C.M.Overall,
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Structure,
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Biol Chem,
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and
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Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9/gelatinase B.
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Structure,
15,
1227-1236.
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J.Hu,
P.E.Van den Steen,
Q.X.Sang,
and
G.Opdenakker
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Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases.
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Nat Rev Drug Discov,
6,
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L.Pérez,
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Substitution of methionine 435 with leucine, isoleucine, and serine in tumor necrosis factor alpha converting enzyme inactivates ectodomain shedding activity.
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Biochem Cell Biol,
85,
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and
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Humoral and cellular immunity induced by tumor cell vaccine based on the chicken xenogeneic homologous matrix metalloproteinase-2.
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Cancer Gene Ther,
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Y.C.Ip,
S.T.Cheung,
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Atypical localization of membrane type 1-matrix metalloproteinase in the nucleus is associated with aggressive features of hepatocellular carcinoma.
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Mol Carcinog,
46,
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A.G.Remacle,
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and
A.Y.Strongin
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Furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP.
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Oncogene,
25,
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C.L.Sears,
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Clin Genet,
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Chem Biol,
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J Exp Med,
202,
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J Biol Chem,
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|
| |
Proc Natl Acad Sci U S A,
102,
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PDB code:
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M.Björklund,
and
E.Koivunen
(2005).
Gelatinase-mediated migration and invasion of cancer cells.
|
| |
Biochim Biophys Acta,
1755,
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G.Bellon,
L.Martiny,
and
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Matrix metalloproteinases and matrikines in angiogenesis.
|
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Crit Rev Oncol Hematol,
49,
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G.Klein,
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and
E.S.de Bont
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The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia.
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Crit Rev Oncol Hematol,
50,
87.
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I.Svab,
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and
M.L.Flonta
(2004).
Binding affinities for sulfonamide inhibitors with matrix metalloproteinase-2 using a linear response method.
|
| |
J Cell Mol Med,
8,
551-562.
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M.Kondo,
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and
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Anti-neovascular therapy by liposomal drug targeted to membrane type-1 matrix metalloproteinase.
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| |
Int J Cancer,
108,
301-306.
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P.K.Vayalil,
and
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(2004).
Treatment of epigallocatechin-3-gallate inhibits matrix metalloproteinases-2 and -9 via inhibition of activation of mitogen-activated protein kinases, c-jun and NF-kappaB in human prostate carcinoma DU-145 cells.
|
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Prostate,
59,
33-42.
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PDB code:
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J.P.Schanstra,
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PDB code:
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PDB code:
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PDB codes:
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PDB code:
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Citation data come partly from CiteXplore and partly
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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
code is
shown on the right.
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|
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