4cbn
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_4cbn| PDB=4cbn | SCENE= }} | {{STRUCTURE_4cbn| PDB=4cbn | SCENE= }} | ||
===Crystal structure of Complement Factor D mutant R202A after conventional refinement=== | ===Crystal structure of Complement Factor D mutant R202A after conventional refinement=== | ||
+ | {{ABSTRACT_PUBMED_24598742}} | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
[[4cbn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBN OCA]. | [[4cbn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBN OCA]. | ||
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:024598742</ref><references group="xtra"/><references/> | ||
[[Category: Complement factor D]] | [[Category: Complement factor D]] | ||
[[Category: Burnley, B T.]] | [[Category: Burnley, B T.]] |
Revision as of 08:47, 19 March 2014
Contents |
Crystal structure of Complement Factor D mutant R202A after conventional refinement
Template:ABSTRACT PUBMED 24598742
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.
About this Structure
4cbn is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- Forneris F, Burnley BT, Gros P. Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):733-43. doi:, 10.1107/S1399004713032549. Epub 2014 Feb 15. PMID:24598742 doi:http://dx.doi.org/10.1107/S1399004713032549