View source for Matriptase

<StructureSection load='1eax' size='350' side='right' caption='Structure of human matriptase catalytic domain complex with benzamidine and sulfate (PDB code [[1eax]]). ' scene='59/595760/Cv/1'>

== 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<ref>PMID:16838070</ref>.  

== Relevance ==

ST14 has a role in ovarian cancer and is a target for anti-cancer therapy<ref>PMID:12779007</ref>.  Inflammation-associated reactive oxygen species and tissue acidity enhance ST14 activation in some skin diseases<ref>PMID:21123732</ref>.

== Structural highlights ==
ST14 active site has the conformation of a typical serine protease like trypsin or chymotrypsin with the <scene name='59/595760/Cv/5'>Ser-His-Asp catalytic triad</scene> and <scene name='59/595760/Cv/6'>Gly-Ser oxyanion hole</scene>.  The <scene name='59/595760/Cv/7'>inhibitor benzamidine blocks the catalytic triad</scene><ref>PMID:11696548</ref>. Water molecules shown as red spheres.

== 3D Structures of matriptase ==
[[Matriptase 3D structures]]

</StructureSection>

== References ==
<references/>

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