Biology:Complement component 1s
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Short description: Protein found in humans
 Generic protein structure example |
Complement component 1s (EC 3.4.21.42, C1 esterase, activated complement C1s, complement C overbar 1r, C1s) is a protein involved in the complement system. C1s is part of the C1 complex.[1][2][3][4] In humans, it is encoded by the C1S gene.[5]
C1s cleaves C4 and C2, which eventually leads to the production of the classical pathway C3-convertase.
See also
- C1q - another part of the C1 complex
- C1r - another part of the C1 complex
- MASP-2 - a protein similar to C1s, part of the lectin pathway
References
- ↑ "The human complement system serine proteases and their proenzymes". Proteolytic Enzymes, Part C. Methods in Enzymology. 80 Pt C. 1981. pp. 26–42. doi:10.1016/s0076-6879(81)80006-7. ISBN 9780121819804.
- ↑ "Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence". European Journal of Biochemistry 169 (3): 547–53. December 1987. doi:10.1111/j.1432-1033.1987.tb13644.x. PMID 3500856.
- ↑ "Molecular organization and function of the complement system". Annual Review of Biochemistry 57: 321–47. 1988. doi:10.1146/annurev.bi.57.070188.001541. PMID 3052276.
- ↑ "The specificity of two proteinases that cleave adjacent to arginine, C1 esterase and acrosin, for peptide p-nitroanilide substrates". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 996 (1–2): 89–94. June 1989. doi:10.1016/0167-4838(89)90099-x. PMID 2500154.
- ↑ "Entrez Gene: C1S Complement component 1, s subcomponent". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=716.
Further reading
- "Recombinant human complement subcomponent C1s lacking beta-hydroxyasparagine, sialic acid, and one of its two carbohydrate chains still reassembles with C1q and C1r to form a functional C1 complex". Biochemistry 31 (17): 4254–62. May 1992. doi:10.1021/bi00132a015. PMID 1533159.
- "Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-dependent interactions of human C1s. Location of the iodination sites". Biochemistry 30 (29): 7135–41. July 1991. doi:10.1021/bi00243a014. PMID 1854725.
- "Identification of the disulfide bonds of human complement C1s". Biochemistry 30 (11): 2827–33. March 1991. doi:10.1021/bi00225a014. PMID 2007122.
- "Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region". Biochemistry 29 (14): 3570–8. April 1990. doi:10.1021/bi00466a021. PMID 2141278.
- "NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- with C1q". Biochemistry 29 (19): 4613–8. May 1990. doi:10.1021/bi00471a016. PMID 2372546.
- "Human genes for complement components C1r and C1s in a close tail-to-tail arrangement". Proceedings of the National Academy of Sciences of the United States of America 85 (19): 7307–11. October 1988. doi:10.1073/pnas.85.19.7307. PMID 2459702. Bibcode: 1988PNAS...85.7307K.
- "Synthesis and regulation of C1 inhibitor in human skin fibroblasts". Journal of Immunology 142 (6): 2041–5. March 1989. doi:10.4049/jimmunol.142.6.2041. PMID 2537870.
- "Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin". Journal of Molecular Biology 208 (4): 709–14. August 1989. doi:10.1016/0022-2836(89)90161-7. PMID 2553984.
- "Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr". Biochemistry 26 (26): 8516–24. December 1987. doi:10.1021/bi00400a004. PMID 2831944.
- "Assignment of the complement serine protease genes C1r and C1s to chromosome 12 region 12p13". Human Genetics 78 (4): 363–8. April 1988. doi:10.1007/BF00291737. PMID 2834284.
- "Human complement component C1s. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation". European Journal of Biochemistry 156 (1): 49–57. April 1986. doi:10.1111/j.1432-1033.1986.tb09546.x. PMID 3007145.
- "Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence". European Journal of Biochemistry 169 (3): 547–53. December 1987. doi:10.1111/j.1432-1033.1987.tb13644.x. PMID 3500856.
- "Basic proline-rich proteins from human parotid saliva: complete covalent structures of proteins IB-1 and IB-6". Biochemistry 25 (9): 2387–92. May 1986. doi:10.1021/bi00357a013. PMID 3521730.
- "Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization". Biochemistry 25 (15): 4292–301. July 1986. doi:10.1021/bi00363a018. PMID 3756141.
- "The serine proteinase chain of human complement component C1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments". The Biochemical Journal 215 (3): 565–71. December 1983. doi:10.1042/bj2150565. PMID 6362661.
- "Structural and circular-dichroism studies on the interaction between human C1-esterase inhibitor and C1s". The Biochemical Journal 213 (3): 617–24. September 1983. doi:10.1042/bj2130617. PMID 6604523.
- "Structure of the catalytic region of human complement protease C1s: study by chemical cross-linking and three-dimensional homology modeling". Biochemistry 34 (22): 7311–21. June 1995. doi:10.1021/bi00022a004. PMID 7779774.
- "Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family". Biochemistry 37 (5): 1204–14. February 1998. doi:10.1021/bi971851v. PMID 9477945.
- "Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates". Journal of Immunology 161 (9): 4924–30. November 1998. doi:10.4049/jimmunol.161.9.4924. PMID 9794427.
- "Selective complement C1s deficiency caused by homozygous four-base deletion in the C1s gene". Human Genetics 103 (4): 415–8. October 1998. doi:10.1007/s004390050843. PMID 9856483.
External links
- Complement+C1s at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human C1S genome location and C1S gene details page in the UCSC Genome Browser.
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