Velcro mechanism (cysteine switch)
An activation mechanism for matrix metalloproteinase family zymogens (named in reference to the zipper-type mechanism), in which the thiol group of a cysteine residue in the N-terminal propart binds to and blocks the active-site Zn atom so that activation occurs when the thiol group is itself blocked, e.g. by N-ethylmaleimide or a heavy metal, or when the propart is proteolytically excised. (see also peptide Velcro)Vallee, B.L. and Auld, D.S. (1990) Biochemistry 29, 5647-5659; Van Wart, H.E. and Birkedal-Hansen, H. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 5578-5582
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