Matriptase
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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3D Structures of matriptase
Updated on 28-October-2019
- matriptase
- Matriptase 3D structures, 5lyo – hST14 catalytic domain - human
- Matriptase 3D structures, 5lyo – hST14 catalytic domain - human
- Matriptase complex with small molecule inhibitor
- 1eax – hST14 catalytic domain + benzamidine
- 3p8g – hST14 residues 182-422 (mutant) + benzamidine
- 2gv6 – hST14 catalytic domain + benzamidine derivative
- 4o97, 4o9v – hST14 catalytic domain + benzamidine derivative + tetrapeptide
- 3ncl – hST14 catalytic domain (mutant) + benzamidine derivative
- 2gv7, 4jz1, 4jzi, 4jyt, 4r0i – hST14 catalytic domain + inhibitor
- 6n4t – hST14 catalytic domain + benzothiazole derivative
- 1eax – hST14 catalytic domain + benzamidine
- Matriptase complex with polypeptide inhibitor