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| Line 12: |
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| *<scene name='46/465445/Cv/12'>K ion coordination site</scene>. Water molecules are shown as red spheres. | | *<scene name='46/465445/Cv/12'>K ion coordination site</scene>. Water molecules are shown as red spheres. |
| *<scene name='46/465445/Cv/13'>Cl ion coordination site I</scene>. | | *<scene name='46/465445/Cv/13'>Cl ion coordination site I</scene>. |
| *<scene name='46/465445/Cv/8'>Cl ion coordination site II</scene>. | | *<scene name='46/465445/Cv/14'>Cl ion coordination site II</scene>. |
| *<scene name='46/465445/Cv/9'>Cl ion coordination site III</scene>. | | *<scene name='46/465445/Cv/15'>Cl ion coordination site III</scene>. |
| *<scene name='46/465445/Cv/10'>Cl ion coordination site IV</scene>. | | *<scene name='46/465445/Cv/16'>Cl ion coordination site IV</scene>. |
| </StructureSection> | | </StructureSection> |
| == 3D Structures of plasminogen == | | == 3D Structures of plasminogen == |
Revision as of 12:38, 8 August 2019
| 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.
- Microplasmin induces posterior vitreous detachment from the retina (PVD)[1].
Disease
PLN mutations are associated with ligneous conjunctivitis and other disorders which lead to development of pseudo membranes on mucosal surfaces[2].
Structural highlights
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, e.g. Kringle 4. The kringle domain is important in protein-protein interaction with blood coagulation factors.[3].
- ↑ Goldenberg DT, Giblin FJ, Cheng M, Chintala SK, Trese MT, Drenser KA, Ruby AJ. Posterior vitreous detachment with microplasmin alters the retinal penetration of intravitreal bevacizumab (Avastin) in rabbit eyes. Retina. 2011 Feb;31(2):393-400. doi: 10.1097/IAE.0b013e3181e586b2. PMID:21099453 doi:https://dx.doi.org/10.1097/IAE.0b013e3181e586b2
- ↑ 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:https://dx.doi.org/10.1111/j.1365-2516.2008.01825.x
- ↑ Law RH, Caradoc-Davies T, Cowieson N, Horvath AJ, Quek AJ, Encarnacao JA, Steer D, Cowan A, Zhang Q, Lu BG, Pike RN, Smith AI, Coughlin PB, Whisstock JC. The X-ray crystal structure of full-length human plasminogen. Cell Rep. 2012 Mar 29;1(3):185-90. doi: 10.1016/j.celrep.2012.02.012. Epub 2012, Mar 8. PMID:22832192 doi:10.1016/j.celrep.2012.02.012
|
3D Structures of plasminogen
Updated on 08-August-2019
{"openlevels":0}
- Plasminogen
- 4dur, 4duu, 4a5t – hPLG 2 residues 20-810 - human
- 2kj4 – hPLG residues 1-83 + M2 protein peptide – NMR
- Plasminogen kringle 1 residues 101-181
- 1pkr - hPLG kringle 1
- 1cea - hPLG kringle 1 + e-aminocaprioic acid
- 1hpj, 1hpk - hPLG kringle 1 + 6-aminohexanoic acid - NMR
- 1ceb - hPLG kringle 1 + AMCHA
- 4cik - hPLG kringle 1 + inhibitor
- Plasminogen kringle 2 residues 181-263
- 1b2i - hPLG kringle 2 (mutant) – NMR
- 1i5k - hPLG kringle 2 (mutant) + M2 protein peptide
- Plasminogen kringle 3 resides 272-354
- 2l0s - hPLG kringle 3 – NMR
- Plasminogen kringle 4 resides 375-454
- Plasminogen kringle 5 resides 480-563
- 5hpg - hPLG kringle 5
- 2knf - hPLG kringle 5 – NMR
- Plasminogen catalytic domain residues 543-791
- 1qrz, 1ddj, 1rjx – hPLG catalytic domain (mutant)
- 1l4d, 1l4z - hPLG catalytic domain (mutant) + streptokinase α domain
- Plasmin
- 1bml – hPLN catalytic domain + streptokinase
- 1bui – hPLN light chain + staphylokinase
- Microplasmin
References
