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4os6

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==Crystal structure of urokinase-type plasminogen activator (uPA) complexed with bicyclic peptide UK604 (bicyclic 2)==
==Crystal structure of urokinase-type plasminogen activator (uPA) complexed with bicyclic peptide UK604 (bicyclic 2)==
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<StructureSection load='4os6' size='340' side='right' caption='[[4os6]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='4os6' size='340' side='right'caption='[[4os6]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4os6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OS6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4os6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OS6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=81R:(4R)-4,5-DISULFANYL-L-NORVALINE'>81R</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=81R:(4R)-4,5-DISULFANYL-L-NORVALINE'>81R</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4os6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4os6 OCA], [https://pdbe.org/4os6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4os6 RCSB], [https://www.ebi.ac.uk/pdbsum/4os6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4os6 ProSAT]</span></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gly|4gly]], [[4os1|4os1]], [[4os2|4os2]], [[4os4|4os4]], [[4os5|4os5]], [[4os7|4os7]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/U-plasminogen_activator U-plasminogen activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.73 3.4.21.73] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4os6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4os6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4os6 RCSB], [http://www.ebi.ac.uk/pdbsum/4os6 PDBsum]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN]] Defects in PLAU are the cause of Quebec platelet disorder (QPD) [MIM:[http://omim.org/entry/601709 601709]]. QPD is an autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins.<ref>PMID:20007542</ref>
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[https://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN] Defects in PLAU are the cause of Quebec platelet disorder (QPD) [MIM:[https://omim.org/entry/601709 601709]. QPD is an autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins.<ref>PMID:20007542</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN]] Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
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[https://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN] Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4os6" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Plasminogen activator|Plasminogen activator]]
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*[[Urokinase 3D Structures|Urokinase 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: U-plasminogen activator]]
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[[Category: Homo sapiens]]
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[[Category: Chen, S]]
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[[Category: Large Structures]]
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[[Category: Heinis, C]]
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[[Category: Chen S]]
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[[Category: Pojer, F]]
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[[Category: Heinis C]]
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[[Category: Bicyclic peptide]]
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[[Category: Pojer F]]
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[[Category: Cyclization]]
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[[Category: Disulfide bridge]]
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[[Category: Extracellular]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Inhibitor]]
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[[Category: Protease]]
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Current revision

Crystal structure of urokinase-type plasminogen activator (uPA) complexed with bicyclic peptide UK604 (bicyclic 2)

PDB ID 4os6

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