1xwe: Difference between revisions
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===NMR Structure of C345C (NTR) domain of C5 of complement=== | ===NMR Structure of C345C (NTR) domain of C5 of complement=== | ||
{{ABSTRACT_PUBMED_15598652}} | {{ABSTRACT_PUBMED_15598652}} | ||
==Disease== | |||
[[http://www.uniprot.org/uniprot/CO5_HUMAN CO5_HUMAN]] Defects in C5 are the cause of complement component 5 deficiency (C5D) [MIM:[http://omim.org/entry/609536 609536]]. A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Note=An association study of C5 haplotypes and genotypes in individuals with chronic hepatitis C virus infection shows that individuals homozygous for the C5_1 haplotype have a significantly higher stage of liver fibrosis than individuals carrying at least 1 other allele (PubMed:15995705). | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/CO5_HUMAN CO5_HUMAN]] Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled. Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. C5a also stimulates the locomotion of polymorphonuclear leukocytes (chemokinesis) and direct their migration toward sites of inflammation (chemotaxis). | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:015598652</ref><references group="xtra"/> | <ref group="xtra">PMID:015598652</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Barlow, P N.]] | [[Category: Barlow, P N.]] | ||
Revision as of 05:55, 25 March 2013
NMR Structure of C345C (NTR) domain of C5 of complementNMR Structure of C345C (NTR) domain of C5 of complement
Template:ABSTRACT PUBMED 15598652
DiseaseDisease
[CO5_HUMAN] Defects in C5 are the cause of complement component 5 deficiency (C5D) [MIM:609536]. A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Note=An association study of C5 haplotypes and genotypes in individuals with chronic hepatitis C virus infection shows that individuals homozygous for the C5_1 haplotype have a significantly higher stage of liver fibrosis than individuals carrying at least 1 other allele (PubMed:15995705).
FunctionFunction
[CO5_HUMAN] Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled. Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. C5a also stimulates the locomotion of polymorphonuclear leukocytes (chemokinesis) and direct their migration toward sites of inflammation (chemotaxis).
About this StructureAbout this Structure
1xwe is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.
ReferenceReference
- ↑ Bramham J, Thai CT, Soares DC, Uhrin D, Ogata RT, Barlow PN. Functional insights from the structure of the multifunctional C345C domain of C5 of complement. J Biol Chem. 2005 Mar 18;280(11):10636-45. Epub 2004 Dec 14. PMID:15598652 doi:http://dx.doi.org/10.1074/jbc.M413126200