6rus

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<StructureSection load='6rus' size='340' side='right'caption='[[6rus]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='6rus' size='340' side='right'caption='[[6rus]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6rus]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RUS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6rus]] 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=6RUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RUS 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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=6rus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rus OCA], [http://pdbe.org/6rus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rus RCSB], [http://www.ebi.ac.uk/pdbsum/6rus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rus ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6rus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rus OCA], [https://pdbe.org/6rus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rus RCSB], [https://www.ebi.ac.uk/pdbsum/6rus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rus ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/PROP_HUMAN PROP_HUMAN]] Defects in CFP are the cause of properdin deficiency (PFD) [MIM:[http://omim.org/entry/312060 312060]]. PFD results in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III).<ref>PMID:8871668</ref> <ref>PMID:9710744</ref> <ref>PMID:10909851</ref>
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[https://www.uniprot.org/uniprot/PROP_HUMAN PROP_HUMAN] Defects in CFP are the cause of properdin deficiency (PFD) [MIM:[https://omim.org/entry/312060 312060]. PFD results in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III).<ref>PMID:8871668</ref> <ref>PMID:9710744</ref> <ref>PMID:10909851</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PROP_HUMAN PROP_HUMAN]] A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.
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[https://www.uniprot.org/uniprot/PROP_HUMAN PROP_HUMAN] A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.
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==See Also==
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*[[Complement factor 3D structures|Complement factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Andersen, G R]]
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[[Category: Andersen GR]]
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[[Category: Pedersen, D V]]
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[[Category: Pedersen DV]]
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[[Category: Complement]]
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[[Category: Immune system]]
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[[Category: Innate immunity]]
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[[Category: Protease]]
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[[Category: Regulator]]
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Current revision

Structure of a functional properdin monomer

PDB ID 6rus

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