1hfd
From Proteopedia
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{{STRUCTURE_1hfd| PDB=1hfd | SCENE= }} | {{STRUCTURE_1hfd| PDB=1hfd | SCENE= }} | ||
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===HUMAN COMPLEMENT FACTOR D IN A P21 CRYSTAL FORM=== | ===HUMAN COMPLEMENT FACTOR D IN A P21 CRYSTAL FORM=== | ||
| + | {{ABSTRACT_PUBMED_9753554}} | ||
| + | ==Disease== | ||
| + | [[http://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN]] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:[http://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== | |
| - | + | [[http://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. | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1hfd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFD OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:009753554</ref><references group="xtra"/><references/> |
[[Category: Complement factor D]] | [[Category: Complement factor D]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: Self-regulation]] | [[Category: Self-regulation]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:50:28 2009'' | ||
Revision as of 17:13, 24 March 2013
Contents |
HUMAN COMPLEMENT FACTOR D IN A P21 CRYSTAL FORM
Template:ABSTRACT PUBMED 9753554
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
1hfd is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Jing H, Babu YS, Moore D, Kilpatrick JM, Liu XY, Volanakis JE, Narayana SV. Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity. J Mol Biol. 1998 Oct 9;282(5):1061-81. PMID:9753554 doi:10.1006/jmbi.1998.2089
