Abstract
The kinetic analysis of the inhibition of matrix metalloproteinases by tissue inhibitor of metalloproteinases (TIMP) yields valuable information on the mechanism and specificity of the TIMPs. When combined with the use of genetic engineering or chemical methods of modification to alter specifically the structure of either enzyme or inhibitor, kinetic techniques can also be used to identify the contribution of individual amino acid residues to binding and complex stabilization. Nuclear magnetic resonance (NMR) and crystallographic structures of TIMP-enzyme complexes show that the binding region is very large, covering about 1300Å2, and consists of six separate polypeptide segments of TIMP-1 (1). Thus, a systematic approach to modifying residues at the enzyme-TIMP interface can identify the important features of such a large binding site.
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Hutton, M., Willenbrock, F. (2001). Kinetic Analysis of the Inhibition of Matrix Metalloproteinases by Tissue Inhibitor of Metalloproteinases (TIMP). In: Clark, I.M. (eds) Matrix Metalloproteinase Protocols. Methods in Molecular Biology™, vol 151. Humana Press. https://doi.org/10.1385/1-59259-046-2:519
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DOI: https://doi.org/10.1385/1-59259-046-2:519
Publisher Name: Humana Press
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