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Literature summary for 3.4.21.41 extracted from

  • Illy, C.; Thielens, N.M.; Arlaud, G.J.
    Chemical characterization and location of ionic interactions involved in the assembly of the C1 complex of human complement (1993), J. Protein Chem., 12, 771-781.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
complement component C1s Homo sapiens binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar, which in turn activates C1s, thereby initiating the classical pathway of complement ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
complement component C1s binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar, which in turn activates C1s, thereby initiating the classical pathway of complement Homo sapiens ?
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 ?

Subunits

Subunits Comment Organism
More the C1 complex comprises two loosely interacting subunits, C1q and the Ca2+-dependent C1s-C1r-C1r-C1s tetramer. Binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar, which in turn activates C1s, thereby initiating the classical pathway of complement Homo sapiens