Matriptase: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
<StructureSection load='1eax' size='350' side='right' caption='Structure of human matriptase catalytic domain | <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 == | == Function == | ||
| Line 10: | Line 10: | ||
== 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 catalytic triad<ref>PMID:11696548</ref>. | ST14 active site has the conformation of a typical serine protease like trypsin or chymotrypsin with the <scene name='59/595760/Cv/2'>Ser-His-Asp catalytic triad</scene> and <scene name='59/595760/Cv/3'>Gly-Ser oxyanion hole</scene>. The <scene name='59/595760/Cv/4'>inhibitor benzamidine blocks the catalytic triad</scene><ref>PMID:11696548</ref>. Water molecules shown as red spheres. | ||
</StructureSection> | </StructureSection> | ||
