Structural properties of matrix metalloproteinases
| Autor: | Frank Grams, Wolfram Bode, Hideaki Nagase, Carlos Fernandez-Catalan, Klaus Maskos, Harald Tschesche |
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| Rok vydání: | 1999 |
| Předmět: |
tissue inhibitors of
drug design Protein Conformation Stereochemistry Molecular Sequence Data Arthritis Matrix metalloproteinase matrix metalloproteinases (MMPs) Extracellular matrix crystal structures proteinases Cellular and Molecular Neuroscience Protein structure Hemopexin Catalytic Domain medicine Animals Humans Amino Acid Sequence Molecular Biology Peptide sequence Pharmacology Extracellular Matrix Proteins Chemistry metalloproteinases (TIMPs) Metalloendopeptidases Tissue Inhibitor of Metalloproteinases Cell Biology medicine.disease Cell biology Molecular Medicine Extracellular Matrix Degradation |
| Zdroj: | Cellular and Molecular Life Sciences (CMLS). 55:639-652 |
| ISSN: | 1420-9071 1420-682X |
| DOI: | 10.1007/s000180050320 |
| Popis: | Matrix metalloproteinases (MMPs) are involved in extracellular matrix degradation. Their proteolytic activity must. be precisely regulated by their endogenous protein inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Disruption of this balance results in serious diseases such as arthritis, tumour growth and metastasis. Knowledge of the tertiary structures of the proteins involved is crucial for understanding their functional properties and interference with associated dysfunctions. Within the last few years, several three-dimensional MMP and MMP-TIMP structures became available, showing the domain organization, polypeptide fold and main specificity determinants. Complexes of the catalytic MMP domains with various synthetic inhibitors enabled the structure-based design and improvement of high-affinity ligands, which might be elaborated into drugs. A multitude of reviews surveying work done on all aspects of MMPs have appeared in recent years, but none of them has focused on the three-dimensional structures. This review was written to close the gap. |
| Databáze: | OpenAIRE |
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