Plasminogen: Difference between revisions

Latest revision as of 09:07, 24 November 2019

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Human glycosylated plasminogen complex with acetate, bicarbonate, K+ (purple) and Cl- (green) ions (PDB entry 4dur)

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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].

K ion coordination site. Water molecules are shown as red spheres.
Cl ion coordination site I.
Cl ion coordination site II.
Cl ion coordination site III.
Cl ion coordination site IV.

3D Structures of plasminogen

Plasminogen 3D structures

↑ 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

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] 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

[2] 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

[3] 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

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@@ Line 1: / Line 1: @@
+<StructureSection load='' size='350' side='right' caption='Human glycosylated plasminogen complex with acetate, bicarbonate, K+ (purple) and Cl- (green) ions (PDB entry [[4dur]])' scene='46/465445/Cv/1'>
-<StructureSection load='4dur' size='350' side='right' caption='Human glycosylated plasminogen complex with acetate, bicarbonate, K+ and Cl- ions (PDB entry [[4dur]])' scene=''>
 == 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.
@@ Line 10: / Line 9: @@
 == 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>.
+<scene name='46/465445/Cv/11'>PLN contains 7 domains</scene> which are: N-terminal, C-terminal serine protease catalytic domain and 5 kringle domains of ca. 80 residues.  The <scene name='46/465445/Cv/3'>kringle domain folds into a large loop containing 3 disulfide bonds</scene>, ''e.g.'' <scene name='46/465445/Cv/4'>Kringle 4</scene>. The kringle domain is important in protein-protein interaction with blood coagulation factors.<ref>PMID:22832192</ref>.
-</StructureSection>
+*<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/14'>Cl ion coordination site II</scene>.
+*<scene name='46/465445/Cv/15'>Cl ion coordination site III</scene>.
+*<scene name='46/465445/Cv/16'>Cl ion coordination site IV</scene>.
 == 3D Structures of plasminogen ==
+[[Plasminogen 3D structures]]
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+</StructureSection>
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Plasminogen
-**[[4dur]], [[4duu]], [[4a5t]] – hPLG  2 - human
-*Plasminogen kringle 1
-**[[1pkr]] - hPLG kringle 1 <BR />
-**[[1cea]] - hPLG kringle 1 + e-aminocaprioic acid<BR />
-**[[1hpj]], [[1hpk]] - hPLG kringle 1 + 6-aminohexanoic acid - NMR<BR />
-**[[1ceb]] - hPLG kringle 1 + AMCHA<br />
-**[[4cik]] - hPLG kringle 1 + inhibitor<br />
-*Plasminogen kringle 2
-**[[1b2i]] - hPLG kringle 2 (mutant) – NMR<BR />
-**[[1i5k]] - hPLG kringle 2 (mutant) + M2 protein peptide<BR />
-**[[2kj4]] – hPLG kringle 2 + M2 protein peptide – NMR<BR />
-*Plasminogen kringle 3
-**[[2l0s]] - hPLG kringle 3 – NMR<BR />
-*Plasminogen kringle 4
-**[[1pk4]], [[1pmk]], [[1pml]], [[1krn]] – hPLG kringle 4<BR />
-**[[2pk4]] - hPLG kringle 4 + e-aminocaprioic acid
-*Plasminogen kringle 5
-**[[5hpg]] - hPLG kringle 5<BR />
-**[[2knf]] - hPLG kringle 5 – NMR<BR />
-*Plasminogen catalytic domain
-**[[1qrz]], [[1ddj]], [[1rjx]] – hPLG catalytic domain (mutant)<br />
-**[[1l4d]], [[1l4z]] - hPLG catalytic domain (mutant) + streptokinase α domain
-*Plasmin
-**[[1bml]] – hPLN catalytic domain + streptokinase<BR />
-**[[1bui]] – hPLN light chain + staphylokinase
-*Microplasmin
-**[[3uir]] – hPLN + textilinin-1<br />
-}}
 == References ==
 <references/>
 [[Category:Topic Page]]

Plasminogen: Difference between revisions

Latest revision as of 09:07, 24 November 2019

Contents

Function

Disease

Structural highlights

3D Structures of plasminogen

References

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