Plasminogen: Difference between revisions
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<StructureSection load='4dur' size='350' side='right' caption='Human glycosylated plasminogen complex with acetate, bicarbonate, K+ (purple) and Cl- (green) ions (PDB entry [[4dur]])' scene=''> | |||
<StructureSection load='4dur' size='350' side='right' caption='Human glycosylated plasminogen complex with acetate, bicarbonate, K+ and Cl- ions (PDB entry [[4dur]])' scene=''> | |||
== Function == | == Function == | ||
'''Plasmin''' (PLN) is a serine protease which is involved in degradation of fibrin clots. PLN is released as the zymogen '''plasminogen''' (PLG) which is converted to the active PLN by a variety of enzymes. PLN cleavage produces angiostatin. | '''Plasmin''' (PLN) is a serine protease which is involved in degradation of fibrin clots. PLN is released as the zymogen '''plasminogen''' (PLG) which is converted to the active PLN by a variety of enzymes. PLN cleavage produces angiostatin. | ||
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== Structural highlights == | == Structural highlights == | ||
PLN contains 7 domains are: N-terminal, C-terminal serine protease catalytic domain and 5 kringle domains of ca. 80 residues. The kringle domain folds into a large loop containing 3 disulfide bonds. The kringle domain is important in protein-protein interaction with blood coagulation factors.<ref>PMID:22832192</ref>. | PLN contains 7 domains which are: N-terminal, C-terminal serine protease catalytic domain and 5 kringle domains of ca. 80 residues. The kringle domain folds into a large loop containing 3 disulfide bonds. The kringle domain is important in protein-protein interaction with blood coagulation factors.<ref>PMID:22832192</ref>. | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of plasminogen == | == 3D Structures of plasminogen == | ||
