Plasminogen
FunctionPlasmin (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.
DiseasePLN mutations are associated with ligneous conjunctivitis and other disorders which lead to development of pseudo membranes on mucosal surfaces[2]. Structural highlightsPLN 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, e.g. Kringle 4. The kringle domain is important in protein-protein interaction with blood coagulation factors.[3].
3D Structures of plasminogen
| ||||||||||||
3D Structures of plasminogen
Updated on 24-November-2019
- Plasminogen
- Plasminogen 3D structures, 4duu, 4a5t – hPLG 2 residues 20-810 - human
- 2kj4 – hPLG residues 1-83 + M2 protein peptide – NMR
- Plasminogen 3D structures, 4duu, 4a5t – hPLG 2 residues 20-810 - human
- Plasminogen kringle 1 residues 101-181
- Plasminogen kringle 2 residues 181-263
- Plasminogen kringle 3 resides 272-354
- 2l0s - hPLG kringle 3 – NMR
- 2l0s - hPLG kringle 3 – NMR
- Plasminogen kringle 4 resides 375-454
- Plasminogen kringle 5 resides 480-563
- Plasminogen catalytic domain residues 543-791
- Plasmin
- Microplasmin