Plasminogen activator

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{{STRUCTURE_1a5h| PDB=1a5h | SIZE=400| SCENE= |right| CAPTION=Human tissue plasminogen activator dimer complex with benzamidine, [[1a5h]] }}
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<StructureSection load='' size='350' side='right' caption='Human tissue plasminogen activator light chain catalytic domain (sky blue and green), heavy chain catalytic domain fragment (yellow and pink) complex with benzamidine, [[1a5h]]' scene='47/476004/Cv/1' pspeed='8' >
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== Function ==
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'''Plasminogen activator''' (PLA) is a serine protease which converts plasminogen to plasmin. TPA structure contains heavy and light chains (HC, LC). PLA is inhibited by PLA inhibitor 1 and 2.
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'''Plasminogen activator''' (PLA) is a serine protease which converts plasminogen to plasmin. It includes Tissue PLA (TPA) which is involved in breakdown of blood clots and urokinase-type PLA [[Urokinase]]. TPA structure contains heavy and light chains (HC, LC). PLA is inhibited by PLA inhibitor 1 and 2.
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*'''Tissue PLA''' (TPA) which is involved in breakdown of blood clots.
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*'''Urokinase-type PLA''' see [[Urokinase]].<br />
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*'''Coagulase/fibrinolysin''' is a plasminogen activator from ''Yersinia pestis'' which possesses coagulase activity is responsible for degradation of plasmid-coded outer membrane proteins<ref>PMID:2843471</ref>.
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{{TOC limit|limit=2}}
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== Relevance ==
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Treatment with tissue PLA for acute ischemic stroke is beneficial<ref>PMID:7477192</ref>.
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== Structural highlights ==
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*<scene name='47/476004/Cv/4'>Interactions between tissue plasminogen activator light chain catalytic domain and heavy chain catalytic domain fragment</scene>. Water molecules are shown as red spheres.
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*<scene name='47/476004/Cv/5'>Benzamidine binding site</scene>.
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</StructureSection>
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==3D structures of plasminogen activator==
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===3D structures of plasminogen activator===
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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[[1a5i]] – PLA residues 213-477 + EGR-CMK – Vampire bat<br />
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*Plasminogen activator
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[[1bqy]] – PLA – Pit viper
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**[[1a5i]] – PLA residues 213-477 + EGR-CMK – Vampire bat<br />
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**[[1bqy]] – PLA – Pit viper
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==Tissue plasminogen activator==
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*Tissue plasminogen activator; Domains – fibrin-binding 36-85; kringle 1 69-153; kringle 2 209-298; catalytic 311-561
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**[[1a5h]] – hTPA HC+LC + benzamidine – human<br />
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**[[1rtf]] - hTPA HC+LC<br />
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**[[1tpg]] – hTPA F1-G - NMR<br />
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**[[1pk2]] – hTPA kringle 2 domain + 6-aminohexanoic acid – NMR<br />
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**[[1tpk]], [[1pml]] - hTPA kringle 2 domain<br />
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**[[1kdu]] - hTPA kringle 1 domain – NMR<br />
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**[[1tpm]], [[1tpn]] - hTPA fibrin-binding domain – NMR<br />
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**[[1bda]] – hTPA catalytic domain (mutant) + EGR-CMK<br />
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**[[5brr]], [[5zlz]] - hTPA catalytic domain (mutant) + plasminogen activator inhibitor 1<br />
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*Coagulase/fibrinolysin
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[[1a5h]] – hTPA HC+LC + benzamidine – human<br />
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**[[2x55]], [[2x56]] - YpTPA – ''Yersinia pestis''<br />
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[[1rtf]] - hTPA HC+LC<br />
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**[[2x4m]] - YpTPA (mutant)<br />
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[[1tpg]] – hTPA F1-G - NMR<br />
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**[[4dcb]] - YpTPA (mutant) + plasminogen peptide<br />
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[[1bda]] – hTPA catalytic domain (mutant) + EGR-CMK<br />
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[[1pk2]] – hTPA kringle 2 domain + 6-aminohexanoic acid – NMR<br />
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[[1tpk]] - hTPA kringle 2 domain<br />
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[[1tpm]], [[1tpn]] - hTPA fibrin-binding domain – NMR
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==Urokinase-type plasminogen activator [[Urokinase]]==
 
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*Urokinase-type plasminogen activator see [[Urokinase]]
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}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human tissue plasminogen activator light chain catalytic domain (sky blue and green), heavy chain catalytic domain fragment (yellow and pink) complex with benzamidine, 1a5h

Drag the structure with the mouse to rotate

3D structures of plasminogen activator

Updated on 21-July-2024


References

  1. Sodeinde OA, Sample AK, Brubaker RR, Goguen JD. Plasminogen activator/coagulase gene of Yersinia pestis is responsible for degradation of plasmid-encoded outer membrane proteins. Infect Immun. 1988 Oct;56(10):2749-52. PMID:2843471
  2. . Tissue plasminogen activator for acute ischemic stroke. The National Institute of Neurological Disorders and Stroke rt-PA Stroke Study Group. N Engl J Med. 1995 Dec 14;333(24):1581-7. PMID:7477192 doi:http://dx.doi.org/10.1056/NEJM199512143332401

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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