Loretta Aureli, Magda Gioia, Ilaria Cerbara, Susanna Monaco, Giovanni Francesco Fasciglione, Stefano Marini, Paolo Ascenzi, Alessandra Topai and Massimo Coletta Pages 2192 - 2222 ( 31 )
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases which are involved in the proteolytic processing of several components of the extracellular matrix. As a consequence, MMPs are implicated in several physiological and pathological processes, like skeletal growth and remodelling, wound healing, cancer, arthritis, and multiple sclerosis, raising a very widespread interest toward this class of enzymes as potential therapeutic targets. Here, structure-function relationships are discussed to highlight the role of different MMP domains on substrate/inhibitor recognition and processing and to attempt the formulation of advanced guidelines, based on natural substrates, for the design of inhibitors more efficient in vivo.
Matrix metalloproteinases,Enzyme-substrate recognition,Enzyme-inhibitor recognition,Structural bases
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