Urokinase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='450' side='right' caption='Human urokinase short chain and catalytic domain complex with inhibitor and phosphate, [[3ig6]]' scene='46/465442/Cv/6' > |
== Function == | == Function == | ||
'''Urokinase''' (UK) or '''urokinase plasminogen activator''' 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). | '''Urokinase''' (UK) or '''urokinase plasminogen activator''' 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). | ||
Revision as of 03:31, 16 October 2017
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3D Structures of urokinase
Updated on 16-October-2017
References
- ↑ 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
- ↑ Han B, Nakamura M, Mori I, Nakamura Y, Kakudo K. Urokinase-type plasminogen activator system and breast cancer (Review). Oncol Rep. 2005 Jul;14(1):105-12. PMID:15944776
- ↑ West CW, Adler M, Arnaiz D, Chen D, Chu K, Gualtieri G, Ho E, Huwe C, Light D, Phillips G, Pulk R, Sukovich D, Whitlow M, Yuan S, Bryant J. Identification of orally bioavailable, non-amidine inhibitors of Urokinase Plasminogen Activator (uPA). Bioorg Med Chem Lett. 2009 Oct 1;19(19):5712-5. Epub 2009 Aug 7. PMID:19703768 doi:10.1016/j.bmcl.2009.08.008
