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Solution structure of wild-type human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor

Michelle A Markus1, Brian Dwyer, Scott Wolfrom

  • 1Structural Biology and Computational Chemistry, Chemical and Screening Sciences, Wyeth Research, 87 Cambridge Park Drive, Cambridge, MA 02140, USA. mmarkus@wyeth.com

Journal of Biomolecular NMR
|April 22, 2008
PubMed
Abstract

No abstract available in PubMed .

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Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
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