Matriptase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <StructureSection load=' | + | <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 == | ||
| Line 12: | Line 12: | ||
== 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
| |||||||||||
3D Structures of matriptase
Updated on 19-April-2016
References
- ↑ Friedrich R, Fuentes-Prior P, Ong E, Coombs G, Hunter M, Oehler R, Pierson D, Gonzalez R, Huber R, Bode W, Madison EL. Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase. J Biol Chem. 2002 Jan 18;277(3):2160-8. Epub 2001 Nov 5. PMID:11696548 doi:10.1074/jbc.M109830200
