6vmj: Difference between revisions

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====
==Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12==
<StructureSection load='6vmj' size='340' side='right'caption='[[6vmj]]' scene=''>
<StructureSection load='6vmj' size='340' side='right'caption='[[6vmj]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
<table><tr><td colspan='2'>[[6vmj]] is a 12 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=6VMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VMJ FirstGlance]. <br>
</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=6vmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vmj OCA], [https://pdbe.org/6vmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vmj RCSB], [https://www.ebi.ac.uk/pdbsum/6vmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vmj ProSAT]</span></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]] 2.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=6vmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vmj OCA], [https://pdbe.org/6vmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vmj RCSB], [https://www.ebi.ac.uk/pdbsum/6vmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vmj ProSAT]</span></td></tr>
</table>
</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__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Z-disk]]
[[Category: Eigenbrot C]]
[[Category: Harris SF]]
[[Category: Wu P]]

Revision as of 11:15, 11 October 2023

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

6vmj is a 12 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.95Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CFAD_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.

Function

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

6vmj, resolution 2.95Å

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