Matriptase
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FunctionMatriptase or suppressor of tumorigenicity 14 protein (ST14) is an epithelial-derived, membrane multi-domain serine protease. ST14 cleaves and activates hepatocyte growth factor/scatter factor and urokinase plasminogen. Benzamidine is an inhibitor of ST14. ST14 catalytic domain contains residues 615-855[1]. RelevanceST14 has a role in ovarian cancer and is a target for anti-cancer therapy[2]. Inflammation-associated reactive oxygen species and tissue acidity enhance ST14 activation in some skin diseases[3]. Structural highlightsST14 active site has the conformation of a typical serine protease like trypsin or chymotrypsin with the Ser-His-Asp catalytic triad and Gly-Ser oxyanion hole. The inhibitor benzamidine blocks the catalytic triad[4]. Water molecules shown as red spheres. 3D Structures of matriptase
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This page was last modified 10:42, 28 October 2019.