6vmk: Difference between revisions
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New page: '''Unreleased structure''' The entry 6vmk is ON HOLD Authors: Wu, P., Harris, S.F., Eigenbrot, C. Description: Crystal structure of human Complement Factor D with anti-Factor D Fab 20D... |
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==Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12== | |||
<StructureSection load='6vmk' size='340' side='right'caption='[[6vmk]], [[Resolution|resolution]] 3.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6vmk]] is a 48 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=6VMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VMK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6vmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vmk OCA], [https://pdbe.org/6vmk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vmk RCSB], [https://www.ebi.ac.uk/pdbsum/6vmk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vmk ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:[https://omim.org/entry/613912 613912]. CFDD is an immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN] Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway. | |||
==See Also== | |||
*[[Complement factor 3D structures|Complement factor 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Wu | [[Category: Eigenbrot C]] | ||
[[Category: Harris SF]] | |||
[[Category: Wu P]] | |||
Latest revision as of 10:09, 3 April 2024
Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12
Structural highlights
DiseaseCFAD_HUMAN Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:613912. CFDD is an immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway. FunctionCFAD_HUMAN Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway. See Also |
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