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}
}
  • C. Fernández-Catalán, W. Bode, +5 authors K. Maskos
  • Published 1998
  • Biology, Medicine
  • The EMBO Journal
    • 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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