Matriptase: Difference between revisions

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<StructureSection load='4isn' size='340' side='right' caption='Structure of human matriptase catalytic domain (grey) complex with Kunitz-type protease inhibitor (green) and glutathione (PDB code [[4isn]]). ' scene=''>
<StructureSection load='1eax' size='340' side='right' caption='Structure of human matriptase catalytic domain (grey) complex with Kunitz-type protease inhibitor (green) and glutathione (PDB code [[4isn]]). ' scene=''>


== Function ==
== Function ==
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== Structural highlights ==
== 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 cataytic triad<ref>PMID:11696548</ref>.
</StructureSection>
</StructureSection>



Revision as of 06:59, 19 April 2016

Structure of human matriptase catalytic domain (grey) complex with Kunitz-type protease inhibitor (green) and glutathione (PDB code 4isn).

Drag the structure with the mouse to rotate

3D Structures of matriptase

Updated on 19-April-2016

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky