Structural Bases for Substrate and Inhibitor Recognition by Matrix Metalloproteinases

Author(s): Loretta Aureli, Magda Gioia, Ilaria Cerbara, Susanna Monaco, Giovanni Francesco Fasciglione, Stefano Marini, Paolo Ascenzi, Alessandra Topai, Massimo Coletta.

Journal Name: Current Medicinal Chemistry

Volume 15 , Issue 22 , 2008

Become EABM
Become Reviewer

Abstract:

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.

Keywords: Matrix metalloproteinases, Enzyme-substrate recognition, Enzyme-inhibitor recognition, Structural bases

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 15
ISSUE: 22
Year: 2008
Page: [2192 - 2222]
Pages: 31
DOI: 10.2174/092986708785747490
Price: $58

Article Metrics

PDF: 4