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* Residue conservation analysis
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Enzyme class:
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Chains A, C:
E.C.3.4.24.17
- stromelysin 1.
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Reaction:
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Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
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Cofactor:
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Ca(2+); Zn(2+)
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Nature
389:77-81
(1997)
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PubMed id:
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Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
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F.X.Gomis-Rüth,
K.Maskos,
M.Betz,
A.Bergner,
R.Huber,
K.Suzuki,
N.Yoshida,
H.Nagase,
K.Brew,
G.P.Bourenkov,
H.Bartunik,
W.Bode.
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ABSTRACT
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Matrix metalloproteinases (MMPs) are zinc endopeptidases that are required for
the degradation of extracellular matrix components during normal embryo
development, morphogenesis and tissue remodelling. Their proteolytic activities
are precisely regulated by endogenous tissue inhibitors of metalloproteinases
(TIMPs). Disruption of this balance results in diseases such as arthritis,
atherosclerosis, tumour growth and metastasis. Here we report the crystal
structure of an MMP-TIMP complex formed between the catalytic domain of human
stromelysin-1 (MMP-3) and human TIMP-1. TIMP-1, a 184-residue protein, has the
shape of an elongated, contiguous wedge. With its long edge, consisting of five
different chain regions, it occupies the entire length of the active-site cleft
of MMP-3. The central disulphide-linked segments Cys 1-Thr 2-Cys 3-Val 4 and Ser
68-Val 69 bind to either side of the catalytic zinc. Cys 1 bidentally
coordinates this zinc, and the Thr-2 side chain extends into the large
specificity pocket of MMP-3. This unusual architecture of the interface between
MMP-3 and TIMP-1 suggests new possibilities for designing TIMP variants and
synthetic MMP inhibitors with potential therapeutic applications.
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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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PDB code:
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H.R.Maun,
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PDB codes:
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P.B.Crowley,
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PDB codes:
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Microsc Res Tech,
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Mol Cancer,
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Dynamic characterisation of the netrin-like domain of human type 1 procollagen C-proteinase enhancer and comparison to the N-terminal domain of tissue inhibitor of metalloproteinases (TIMP).
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Mol Biosyst,
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417-425.
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(2008).
Identification of amino acid residues of the matrix metalloproteinase-2 essential for its selective inhibition by beta-amyloid precursor protein-derived inhibitor.
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Engineered sarafotoxins as tissue inhibitor of metalloproteinases-like matrix metalloproteinase inhibitors.
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and
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S.Atkinson,
and
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Identification of the extracellular matrix (ECM) binding motifs of tissue inhibitor of metalloproteinases (TIMP)-3 and effective transfer to TIMP-1.
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J Biol Chem,
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M.Miyagi,
K.Aoyagi,
S.Kato,
and
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(2007).
The TIMP-1 gene transferred through adenovirus mediation shows a suppressive effect on peritoneal metastases from gastric cancer.
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| |
Int J Clin Oncol,
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and
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(2007).
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| |
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and
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(2007).
General and specific host responses to bacterial infection in Peyer's patches: a role for stromelysin-1 (matrix metalloproteinase-3) during Salmonella enterica infection.
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and
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(2007).
Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1.
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PDB code:
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R.F.Frausto,
J.K.Whitmire,
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B.Shao,
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Myeloperoxidase inactivates TIMP-1 by oxidizing its N-terminal cysteine residue: an oxidative mechanism for regulating proteolysis during inflammation.
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J Biol Chem,
282,
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H.S.Chi,
J.Chen,
and
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JNK/c-Jun signaling pathway mediates the fluoride-induced down-regulation of MMP-20 in vitro.
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Matrix Biol,
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Targeting proteases: successes, failures and future prospects.
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J.Lin,
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Effect of 3D scaffold and dynamic culture condition on the global gene expression profile of mouse embryonic stem cells.
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Biomaterials,
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X.H.Luo,
H.Xie,
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and
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(2006).
Tissue inhibitor of matrix metalloproteinase-1 suppresses apoptosis of mouse bone marrow stromal cell line MBA-1.
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and
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W.Baumgärtner,
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F.Seeliger,
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U.Deschl,
and
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(2006).
MMP-12, MMP-3, and TIMP-1 are markedly upregulated in chronic demyelinating theiler murine encephalomyelitis.
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J Neuropathol Exp Neurol,
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Matrix metalloproteinases and mesangial remodeling in light chain-related glomerular damage.
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Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzyme.
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J Biol Chem,
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Z.Xie,
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Reactive site mutations in tissue inhibitor of metalloproteinase-3 disrupt inhibition of matrix metalloproteinases but not tumor necrosis factor-alpha-converting enzyme.
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J Biol Chem,
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TIMPs as multifacial proteins.
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Crit Rev Oncol Hematol,
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J Biol Chem,
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Adenovirus-mediated overexpression of tissue inhibitor of metalloproteinases-1 in the liver: efficient protection against T-cell lymphoma and colon carcinoma metastasis.
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and
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(2004).
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Structural and functional uncoupling of the enzymatic and angiogenic inhibitory activities of tissue inhibitor of metalloproteinase-2 (TIMP-2): loop 6 is a novel angiogenesis inhibitor.
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J Biol Chem,
278,
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W.Li,
A.Godzik,
E.W.Howard,
and
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(2003).
A residue in the S2 subsite controls substrate selectivity of matrix metalloproteinase-2 and matrix metalloproteinase-9.
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J Biol Chem,
278,
17158-17163.
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E.Kerkelä,
and
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(2003).
Matrix metalloproteinases in tumor progression: focus on basal and squamous cell skin cancer.
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Exp Dermatol,
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E.Liepinsh,
L.Banyai,
G.Pintacuda,
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L.Patthy,
and
G.Otting
(2003).
NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding.
|
| |
J Biol Chem,
278,
25982-25989.
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PDB code:
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M.H.Lee,
M.Rapti,
and
G.Murphy
(2003).
Unveiling the surface epitopes that render tissue inhibitor of metalloproteinase-1 inactive against membrane type 1-matrix metalloproteinase.
|
| |
J Biol Chem,
278,
40224-40230.
|
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|
|
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|
|
R.E.Feltzer,
J.O.Trent,
and
R.D.Gray
(2003).
Alkaline proteinase inhibitor of Pseudomonas aeruginosa: a mutational and molecular dynamics study of the role of N-terminal residues in the inhibition of Pseudomonas alkaline proteinase.
|
| |
J Biol Chem,
278,
25952-25957.
|
|
|
|
|
|
|
S.Higashi,
and
K.Miyazaki
(2003).
Identification of a region of beta-amyloid precursor protein essential for its gelatinase A inhibitory activity.
|
| |
J Biol Chem,
278,
14020-14028.
|
|
|
|
|
|
|
S.Wei,
Y.Chen,
L.Chung,
H.Nagase,
and
K.Brew
(2003).
Protein engineering of the tissue inhibitor of metalloproteinase 1 (TIMP-1) inhibitory domain. In search of selective matrix metalloproteinase inhibitors.
|
| |
J Biol Chem,
278,
9831-9834.
|
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|
|
|
|
|
S.Wei,
Z.Xie,
E.Filenova,
and
K.Brew
(2003).
Drosophila TIMP is a potent inhibitor of MMPs and TACE: similarities in structure and function to TIMP-3.
|
| |
Biochemistry,
42,
12200-12207.
|
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|
|
|
W.Bode,
and
K.Maskos
(2003).
Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.
|
| |
Biol Chem,
384,
863-872.
|
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|
|
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|
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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
code is
shown on the right.
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