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Cited by 328

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Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with an Inhibitor

Lovejoy, Brett, Cleasby, Anne, Hassell, Anne M., Longley, Kelly, Luther, Michael A., Weigl, Debra, McGeehan, Gerard, McElroy, Andrew B., Drewry, David, Lambert, Millard H., Jordan, Steven R.·1994·Science

Abstract

Collagenase is a zinc-dependent endoproteinase and is a member of the matrix metalloproteinase (MMP) family of enzymes. The MMPs participate in connective tissue remodeling events and aberrant regulation has been associated with several pathologies. The 2.4 angstrom resolution structure of the inhibited enzyme revealed that, in addition to the catalytic zinc, there is a second zinc ion and a calcium ion which play a major role in stabilizing the tertiary structure of collagenase. Despite scant sequence homology, collagenase shares structural homology with two other endoproteinases, bacterial thermolysin and crayfish astacin. The detailed description of protein-inhibitor interactions present in the structure will aid in the design of compounds that selectively inhibit individual members of the MMP family. Such inhibitors will be useful in examining the function of MMPs in pathological processes.

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Metadata

Authors
Lovejoy, B., Cleasby, A., Hassell, A. M., Longley, K., Luther, M. A., Weigl, D., McGeehan, G., McElroy, A. B., Drewry, D., Lambert, M. H., & Jordan, S. R.
Venue
Science
Published
1994-01-21
Volume
263
Issue
5145
Pages
375-377
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2159692814
Cited by
328
References
0
FWCI
19.42
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with an Inhibitor. https://app.cochat.ai/papers/10.1126/science.8278810
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Lovejoy, B., Cleasby, A., Hassell, A. M., Longley, K., Luther, M. A., Weigl, D., McGeehan, G., McElroy, A. B., Drewry, D., Lambert, M. H., & Jordan, S. R. (1994). Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with an Inhibitor. Science. https://doi.org/10.1126/science.8278810

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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