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1.56 Å structure of mature truncated human fibroblast collagenase
Abstract
The X‐ray crystal structure of a 19 kDa active fragment of human fibroblast collagenase has been determined by the multiple isomorphous replacement method and refined at 1.56 Å resolution to an R‐factor of 17.4%. The current structure includes a bound hydroxamate inhibitor, 88 waters and three metal atoms (two zincs and a calcium). The overall topology of the enzyme, comprised of a five stranded β‐sheet and three α‐helices, is similar to the thermolysin‐like metalloproteinases. There are some important differences between the collagenase and thermolysin families of enzymes. The active site zinc ligands are all histidines (His‐218, His‐222, and His‐228). The presence of a second zinc ion in a structural role is a unique feature of the matrix metalloproteinases. The binding properties of the active site cleft are more dependent on the main chain conformation of the enzyme (and substrate) compared with thermolysin. A mechanism of action for peptide cleavage similar to that of thermolysin is proposed for fibroblast collagenase. © 1994 Wiley‐Liss, Inc.
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Citations
Cited by
Analysis of zinc binding sites in protein crystal structures
Alberts, I. L., Nadassy, K., & Wodak, S. J. (1998) · Protein Science · doi:10.1002/pro.5560070805 · Cited by 423
Structural properties of matrix metalloproteinases
Bode, W., Fernandez-Catalan, C., Grams, H. T., & Maskos, H. N. (1999) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s000180050320 · Cited by 329
Discovery of Potent Nonpeptide Inhibitors of Stromelysin Using SAR by NMR
Hajduk, P. J., Sheppard, G., Nettesheim, D. G., Olejniczak, E. T., Shuker, S. B., Meadows, R. P., Steinman, D. H., Carrera, G. M., Marcotte, P. A., Severin, J., et al. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9702778 · Cited by 317
MMP-1: the elder of the family
Pardo, A., & Selman, M. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.06.017 · Cited by 268
Hu, X., & Shelver, W. H. (2003) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(03)00153-0 · Cited by 112
Metadata
- Authors
- Spurlino, J. C., Smallwood, A. M., Carlton, D. D., Banks, T. M., Vavra, K. J., Johnson, J. S., Cook, E. R., Falvo, J., Wahl, R. C., Pulvino, T. A., Wendoloski, J. J., & Smith, D. L.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 1994-06
- Volume
- 19
- Issue
- 2
- Pages
- 98-109
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W2036805996
- Cited by
- 184
- References
- 0
- FWCI
- 9.46
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: 1.56 Å structure of mature truncated human fibroblast collagenase. https://app.cochat.ai/papers/10.1002/prot.340190203
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- Spurlino, J. C., Smallwood, A. M., Carlton, D. D., Banks, T. M., Vavra, K. J., Johnson, J. S., Cook, E. R., Falvo, J., Wahl, R. C., Pulvino, T. A., Wendoloski, J. J., & Smith, D. L. (1994). 1.56 Å structure of mature truncated human fibroblast collagenase. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.340190203
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