1fdp

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[[Image:1fdp.png|left|200px]]
 
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{{STRUCTURE_1fdp| PDB=1fdp | SCENE= }}
{{STRUCTURE_1fdp| PDB=1fdp | SCENE= }}
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===PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D===
===PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D===
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{{ABSTRACT_PUBMED_10022823}}
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==Disease==
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[[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.
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==Function==
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[[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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(as it appears on PubMed at http://www.pubmed.gov), where 10022823 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10022823}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:010022823</ref><references group="xtra"/>
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<ref group="xtra">PMID:010022823</ref><references group="xtra"/><references/>
[[Category: Complement factor D]]
[[Category: Complement factor D]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 20:01, 24 March 2013

Template:STRUCTURE 1fdp

Contents

PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D

Template:ABSTRACT PUBMED 10022823

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

1fdp is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Jing H, Macon KJ, Moore D, DeLucas LJ, Volanakis JE, Narayana SV. Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D. EMBO J. 1999 Feb 15;18(4):804-14. PMID:10022823 doi:10.1093/emboj/18.4.804

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OCA

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