Matriptase

spinqualitylabelsall models Structure of human matriptase catalytic domain (grey) complex with benzamidine and sulfate (PDB code 1eax). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Matriptase 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. Relevance ST14 has a role in ovarian cancer and is a target for anti-cancer therapy. Inflammation-associated reactive oxygen species and tissue acidity enhance ST14 activation in some skin diseases. Structural highlights ST14 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.

3D Structures of matriptase

Updated on 19-April-2016

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• matriptase
  • 4is5 – 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 – hST14 catalytic domain + inhibitor
    
• Matriptase complex with polypeptide inhibitor
  • 1eaw – hST14 catalytic domain + BPTI
    
  • 3bn9 – hST14 catalytic domain + antibody
    
  • 3nps, 3so3 – hST14 catalytic domain (mutant) + antibody
    
  • 3p8f – hST14 residues 182-422 (mutant) + trypsin inhibitor peptide
    
  • 4isl, 4isn, 4iso – hST14 catalytic domain (mutant) + Kunitz-type protease inhibitor
    

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Michal Harel, Alexander Berchansky