Urokinase

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<StructureSection load='1c5w' size='340' side='right' caption='Human urokinase short chain (grey) and catalytic domain (green) complex with iodobenzine inhibitor and citrate, [[1c5w]]' scene='' >
<StructureSection load='1c5w' size='340' side='right' caption='Human urokinase short chain (grey) and catalytic domain (green) complex with iodobenzine inhibitor and citrate, [[1c5w]]' scene='' >
== Function ==
== Function ==
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'''Urokinase''' (UK) is a serine protease whose principal substrate is plasminogen – the inactive zymogen of plasmin<ref>PMID:15454079</ref>. UK consists of 3 domains: ligand-binding domain and kringle and growth factor domains. Prourokinase (PUK) is the inactive zymogen of UK which becomes active by proteolytic cleavage into catalytic domain (residues 179-431) and short chain (residues 156-178).
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'''Urokinase''' (UK) is a serine protease whose principal substrate is plasminogen – the inactive zymogen of plasmin<ref>PMID:21711235</ref>. UK consists of 3 domains: ligand-binding domain and kringle and growth factor domains. Prourokinase (PUK) is the inactive zymogen of UK which becomes active by proteolytic cleavage into catalytic domain (residues 179-431) and short chain (residues 156-178).
</StructureSection>
</StructureSection>
== 3D Structures of urokinase ==
== 3D Structures of urokinase ==

Revision as of 09:11, 11 December 2016

Human urokinase short chain (grey) and catalytic domain (green) complex with iodobenzine inhibitor and citrate, 1c5w

Drag the structure with the mouse to rotate

3D Structures of urokinase

Updated on 11-December-2016

References

  1. Carriero MV, Stoppelli MP. The urokinase-type plasminogen activator and the generation of inhibitors of urokinase activity and signaling. Curr Pharm Des. 2011;17(19):1944-61. PMID:21711235

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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