This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Plasminogen
From Proteopedia
| Line 1: | Line 1: | ||
{{STRUCTURE_1qrz| PDB=1qrz | SIZE=400| SCENE= |right|CAPTION=Human plasmin catalytic domain tetramer, [[1qrz]] }} | {{STRUCTURE_1qrz| PDB=1qrz | SIZE=400| SCENE= |right|CAPTION=Human plasmin catalytic domain tetramer, [[1qrz]] }} | ||
| - | + | == 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. PLN 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. | '''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. PLN 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. | ||
| + | |||
| + | == Disease == | ||
| + | PLN mutations are associated with ligneous conjunctivitis and other disorders which lead to development of pseudo membranes on mucosal surfaces<ref>PMID:19141167</ref>. | ||
== 3D Structures of plasminogen == | == 3D Structures of plasminogen == | ||
| Line 54: | Line 57: | ||
**[[3uir]] – hPLN + textilinin-1<br /> | **[[3uir]] – hPLN + textilinin-1<br /> | ||
}} | }} | ||
| - | + | == References == | |
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:22, 4 July 2016
Contents |
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. PLN 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.
Disease
PLN mutations are associated with ligneous conjunctivitis and other disorders which lead to development of pseudo membranes on mucosal surfaces[1].
3D Structures of plasminogen
Updated on 04-July-2016
References
- ↑ Mehta R, Shapiro AD. Plasminogen deficiency. Haemophilia. 2008 Nov;14(6):1261-8. doi: 10.1111/j.1365-2516.2008.01825.x. PMID:19141167 doi:http://dx.doi.org/10.1111/j.1365-2516.2008.01825.x
