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Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’
Abstract
The X‐ray crystal structures of two zinc endopeptidases, astacin from crayfish, and adamalysin II from snake venom, reveal a strong overall topological equivalence and virtually identical extended HEXXHXXGXXH zinc‐binding segments, but in addition a methionine‐containing turn of similar conformation (the ‘Met‐turn’), which forms a hydrophobic basis for the zinc ion and the three liganding histidine residues. These two features are also present in a similar arrangement in the matrix metalloproteinases (matrixins) and in the large bacterial Serratia proteinase‐like peptidases (serralysins). We suggest that these four proteinases represent members of distinct subfamilies which can be grouped together in a family, for which we propose the designation, metzincins.
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Cited by
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
Structure and function of matrix metalloproteinases and TIMPs
NAGASE, H., VISSE, R., & MURPHY, G. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.12.002 · Cited by 3,409
Matrix metalloproteinases and the regulation of tissue remodelling
Page-McCaw, A., Ewald, A. J., & Werb, Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2125 · Cited by 2,630
Matrix metalloproteinases as modulators of inflammation and innate immunity
Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929
Biochemical and Biological Attributes of Matrix Metalloproteinases
Cui, N., Hu, M., & Khalil, R. A. (2017) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2017.02.005 · Cited by 1,359
Metadata
- Authors
- Bode, W., Gomis-Rüth, F.-X., & Stöckler, W.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1993-09-27
- Volume
- 331
- Issue
- 1-2
- Pages
- 134-140
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2019838731
- Cited by
- 757
- References
- 0
- FWCI
- 12.93
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’. https://app.cochat.ai/papers/10.1016/0014-5793(93)80312-i
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- Bode, W., Gomis-Rüth, F.-X., & Stöckler, W. (1993). Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’. FEBS Letters. https://doi.org/10.1016/0014-5793(93)80312-i
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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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