6sej

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<StructureSection load='6sej' size='340' side='right'caption='[[6sej]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='6sej' size='340' side='right'caption='[[6sej]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6sej]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SEJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6sej]] 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=6SEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SEJ 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></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]] 3.501&#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=6sej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sej OCA], [http://pdbe.org/6sej PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sej RCSB], [http://www.ebi.ac.uk/pdbsum/6sej PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sej 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></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=6sej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sej OCA], [https://pdbe.org/6sej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sej RCSB], [https://www.ebi.ac.uk/pdbsum/6sej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sej 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 54 kDa protein properdin, also known as factor P (FP), plays a major role in the complement system through the stabilization of the alternative pathway convertases. FP circulates in the blood as cyclic dimers, trimers and tetramers, and this heterogeneity challenges detailed structural insight into the mechanism of convertase stabilization by FP. Here, the generation of an intact FP monomer and a variant monomer with the third thrombospondin repeat liberated is described. Both FP monomers were excised from recombinant full-length FP containing internal cleavage sites for TEV protease. These FP monomers could be crystallized, and complete data sets extending to 2.8 A resolution for the intact FP monomer and to 3.5 A resolution for the truncated variant were collected. The principle of specific monomer excision and domain removal by the insertion of a protease cleavage site may be broadly applicable to structural studies of oligomeric, flexible and modular proteins.
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Crystallization and X-ray analysis of monodisperse human properdin.,Pedersen DV, Revel M, Gadeberg TAF, Andersen GR Acta Crystallogr F Struct Biol Commun. 2019 Feb 1;75(Pt 2):0. doi:, 10.1107/S2053230X18018150. Epub 2019 Jan 23. PMID:30713161<ref>PMID:30713161</ref>
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==See Also==
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*[[Complement factor 3D structures|Complement factor 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6sej" style="background-color:#fffaf0;"></div>
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== 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 monomeric properdin lacking TSR3

PDB ID 6sej

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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