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==CRYSTAL STRUCTURE OF PLATELET FACTOR 4 MUTANT 2== | ==CRYSTAL STRUCTURE OF PLATELET FACTOR 4 MUTANT 2== | ||
<StructureSection load='1f9s' size='340' side='right' caption='[[1f9s]], [[Resolution|resolution]] 2.38Å' scene=''> | <StructureSection load='1f9s' size='340' side='right'caption='[[1f9s]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f9s]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1f9s]] is a 4 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=1F9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F9S FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38Å</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f9s OCA], [https://pdbe.org/1f9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f9s RCSB], [https://www.ebi.ac.uk/pdbsum/1f9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f9s ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PLF4_HUMAN PLF4_HUMAN] Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.<ref>PMID:7644496</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f9/1f9s_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f9/1f9s_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f9s ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | |||
*[[C-X-C motif chemokine 3D structures|C-X-C motif chemokine 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Aster | [[Category: Large Structures]] | ||
[[Category: Doyle | [[Category: Aster R]] | ||
[[Category: Edwards | [[Category: Doyle M]] | ||
[[Category: Faulk | [[Category: Edwards B]] | ||
[[Category: Visentin | [[Category: Faulk T]] | ||
[[Category: Yang | [[Category: Visentin G]] | ||
[[Category: Yang J]] | |||
Latest revision as of 10:15, 9 October 2024
CRYSTAL STRUCTURE OF PLATELET FACTOR 4 MUTANT 2CRYSTAL STRUCTURE OF PLATELET FACTOR 4 MUTANT 2
Structural highlights
FunctionPLF4_HUMAN Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences |
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