4os5: Difference between revisions

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 ==Crystal structure of urokinase-type plasminogen activator (uPA) complexed with bicyclic peptide UK603 (bicyclic 2)==
-<StructureSection load='4os5' size='340' side='right' caption='[[4os5]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
+<StructureSection load='4os5' size='340' side='right'caption='[[4os5]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4os5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OS5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OS5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4os5]] 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=4OS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OS5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PRD_001227:bicyclic+peptide+UK603+(bicyclic+2)'>PRD_001227</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4os5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4os5 OCA], [https://pdbe.org/4os5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4os5 RCSB], [https://www.ebi.ac.uk/pdbsum/4os5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4os5 ProSAT]</span></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gly|4gly]], [[4os1|4os1]], [[4os2|4os2]], [[4os4|4os4]], [[4os6|4os6]], [[4os7|4os7]]</td></tr>
-<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>
-<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=4os5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4os5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4os5 RCSB], [http://www.ebi.ac.uk/pdbsum/4os5 PDBsum]</span></td></tr>
 </table>
 == Disease ==
-[[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>
+[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 ==
-[[http://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN]] Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4os5" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Plasminogen activator|Plasminogen activator]]
+*[[Urokinase 3D Structures|Urokinase 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: U-plasminogen activator]]
+[[Category: Homo sapiens]]
-[[Category: Chen, S.]]
+[[Category: Large Structures]]
-[[Category: Heinis, C.]]
+[[Category: Chen S]]
-[[Category: Pojer, F.]]
+[[Category: Heinis C]]
-[[Category: Bicyclic peptide]]
+[[Category: Pojer F]]
-[[Category: Cyclization]]
-[[Category: Disulfide bridge]]
-[[Category: Extracellular]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Inhibitor]]
-[[Category: Protease]]