Urokinase: Difference between revisions
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<StructureSection load='3ig6' size='350' side='right' caption='Human urokinase light chain fragment (pink) and catalytic domain (yellow) complex with inhibitor and phosphate, [[3ig6]]' scene='' > | <StructureSection load='3ig6' size='350' side='right' caption='Human urokinase light chain fragment (pink) and catalytic domain (yellow) complex with inhibitor and phosphate, [[3ig6]]' scene='' > | ||
== 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''' or '''urokinase-type 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). | ||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
The <scene name='46/465442/Cv/10'>inhibitor | The <scene name='46/465442/Cv/10'>inhibitor of UK binds in the active site of UK</scene> and interacts with the active Ser of the catalytic triad<ref>PMID:19703768</ref>. Water molecules are shown as red spheres. | ||
== 3D Structures of urokinase == | == 3D Structures of urokinase == | ||
[[Urokinase 3D Structures]] | [[Urokinase 3D Structures]] | ||
Latest revision as of 11:03, 14 March 2024
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