C3 (complement)

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Complement component 3
PDB rendering based on 1c3d.
Available structures: 1c3d, 1ghq, 1w2s, 2a73, 2a74, 2b39, 2gox, 2hr0, 2i07, 2ice, 2icf
Identifiers
Symbol(s) C3; ASP; CPAMD1
External IDs OMIM: 120700 MGI88227 Homologene68031
Orthologs
Human Mouse
Entrez 718 12266
Ensembl na ENSMUSG00000024164
Uniprot na Q207D2
Refseq NM_000064 (mRNA)
NP_000055 (protein)
NM_009778 (mRNA)
NP_033908 (protein)
Location na Chr 17: 56.89 - 56.91 Mb
Pubmed search [1] [2]

In immunology, soluble C3-convertase, also known as iC3Bb, catalyzes the proteolytic cleavage of C3 into C3a and C3b as part of the alternative complement system.

Contents

C3a plays an important role in chemotaxis, though not as important a role as C5a.[1]

It is also an anaphylatoxin.

C3b may bind to microbial cell surfaces within an organism's body. This can lead to the production of surface-bound C3 convertase and thus more C3b components. Also known as C3bBb, this convertase is similar to soluble C3-convertase except that it is membrane bound.

Alternatively, bound C3b may aid in opsonization of the microbe by macrophages.[1] Complement receptor 1 or CR1 on macrophages allows the engaging of C3b covered microbes.

C3b is cleaved into C3c and C3d.

  1. ^ a b Immunology at MCG 1/phagocyt

  • Sahu A, Lambris J (2001). "Structure and biology of complement protein C3, a connecting link between innate and acquired immunity". Immunol Rev 180: 35-48. PMID 11414361. 
  • Fredslund F, Jenner L, Husted L, Nyborg J, Andersen G, Sottrup-Jensen L (2006). "The structure of bovine complement component 3 reveals the basis for thioester function". J Mol Biol 361 (1): 115-27. PMID 16831446. 
  • PDB 2B39, PDB 2A73
  • domain structure; protein database
  • MeSH Complement+C3

  • Matsuyama W, Nakagawa M, Takashima H, et al. (2002). "Molecular analysis of hereditary deficiency of the third component of complement (C3) in two sisters.". Intern. Med. 40 (12): 1254-8. PMID 11813855. 


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