1oc0: Difference between revisions

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OCA

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 <StructureSection load='1oc0' size='340' side='right'caption='[[1oc0]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1oc0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OC0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OC0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1oc0]] 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=1OC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OC0 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a7c|1a7c]], [[1b3k|1b3k]], [[1c5g|1c5g]], [[1db2|1db2]], [[1dvm|1dvm]], [[1dvn|1dvn]], [[1lj5|1lj5]], [[9pai|9pai]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28&#8491;</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=1oc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oc0 OCA], [http://pdbe.org/1oc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oc0 RCSB], [http://www.ebi.ac.uk/pdbsum/1oc0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oc0 ProSAT]</span></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=1oc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oc0 OCA], [https://pdbe.org/1oc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1oc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oc0 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/PAI1_HUMAN PAI1_HUMAN]] Defects in SERPINE1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:[http://omim.org/entry/613329 613329]]. It is a hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen.<ref>PMID:9207454</ref>   Note=High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.
+[https://www.uniprot.org/uniprot/PAI1_HUMAN PAI1_HUMAN] Defects in SERPINE1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:[https://omim.org/entry/613329 613329]. It is a hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen.<ref>PMID:9207454</ref>   Note=High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.
 == Function ==
-[[http://www.uniprot.org/uniprot/PAI1_HUMAN PAI1_HUMAN]] Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.<ref>PMID:15853774</ref>  [[http://www.uniprot.org/uniprot/VTNC_HUMAN VTNC_HUMAN]] Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.  Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.
+[https://www.uniprot.org/uniprot/PAI1_HUMAN PAI1_HUMAN] Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.<ref>PMID:15853774</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/1oc0_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 37: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Carrell, R W]]
+[[Category: Carrell RW]]
-[[Category: Huntington, J A]]
+[[Category: Huntington JA]]
-[[Category: Pannu, N S]]
+[[Category: Pannu NS]]
-[[Category: Read, R J]]
+[[Category: Read RJ]]
-[[Category: Zhou, A]]
+[[Category: Zhou A]]
-[[Category: Cell adhesion]]
-[[Category: Cell migration]]
-[[Category: Fibrinolysis]]
-[[Category: Heparin-binding]]
-[[Category: Hydrolase-inhibitor complex]]
-[[Category: Plasminogen activation]]
-[[Category: Proteinase inhibitor]]
-[[Category: Serine protease inhibitor-complex]]
-[[Category: Serpin]]