Crystal structure of the complex formed by the membrane type 1‐matrix metalloproteinase with the tissue inhibitor of metalloproteinases‐2, the soluble progelatinase A receptor
@article{FernndezCataln1998CrystalSO, title={Crystal structure of the complex formed by the membrane type 1‐matrix metalloproteinase with the tissue inhibitor of metalloproteinases‐2, the soluble progelatinase A receptor}, author={C. Fern{\'a}ndez-Catal{\'a}n and W. Bode and R. Huber and D. Turk and J. Calvete and A. Lichte and H. Tschesche and K. Maskos}, journal={The EMBO Journal}, year={1998}, volume={17} }
The proteolytic activity of matrix metalloproteinases (MMPs) towards extracellular matrix components is held in check by the tissue inhibitors of metalloproteinases (TIMPs). The binary complex of TIMP‐2 and membrane‐type‐1 MMP (MT1‐MMP) forms a cell surface located ‘receptor’ involved in pro‐MMP‐2 activation. We have solved the 2.75 Å crystal structure of the complex between the catalytic domain of human MT1‐MMP (cdMT1‐MMP) and bovine TIMP‐2. In comparison with our previously determined MMP‐3… CONTINUE READING
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References
SHOWING 1-10 OF 73 REFERENCES
The recombinant catalytic domain of membrane‐type matrix metalloproteinase‐1 (MT1‐MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP‐2
- Chemistry, Medicine
- FEBS letters
- 1996
- 64
Activation of a recombinant membrane type 1‐matrix metalloproteinase (MT1‐MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)‐2
- Chemistry, Medicine
- FEBS letters
- 1996
- 357
- Highly Influential
The X‐ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.
- Biology, Medicine
- The EMBO journal
- 1994
- 257
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
- Biology, Medicine
- Nature
- 1997
- 566
Tissue Inhibitor of Metalloproteinase-2 (TIMP-2) Binds to the Catalytic Domain of the Cell Surface Receptor, Membrane Type 1-Matrix Metalloproteinase 1 (MT1-MMP)*
- Medicine, Biology
- The Journal of Biological Chemistry
- 1998
- 283
- PDF
Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases.
- Chemistry, Medicine
- European journal of biochemistry
- 1997
- 447
- Highly Influential
The Soluble Catalytic Domain of Membrane Type 1 Matrix Metalloproteinase Cleaves the Propeptide of Progelatinase A and Initiates Autoproteolytic Activation
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 1996
- 587
- Highly Influential
- PDF
The TIMP2 Membrane Type 1 Metalloproteinase “Receptor” Regulates the Concentration and Efficient Activation of Progelatinase A
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 1998
- 620
- PDF
Kinetic Analysis of the Binding of Human Matrix Metalloproteinase-2 and -9 to Tissue Inhibitor of Metalloproteinase (TIMP)-1 and TIMP-2*
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 1997
- 275
- PDF
Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions.
- Medicine, Chemistry
- The Journal of biological chemistry
- 1992
- 191
- PDF