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 ==

Latest revision as of 11:03, 14 March 2024

Human urokinase light chain fragment (pink) and catalytic domain (yellow) complex with inhibitor and phosphate, 3ig6

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References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman