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- W54997757 abstract "Publisher Summary The complement system is a mechanism for the recognition of microorganisms that proceeds through two phases, the first being the covalent attachment of two complement system proteins—C3 and C4—to other proteins and to carbohydrates that are part of the complement-activating complex, and the second phase being the receptor-mediated binding of these complexes by various cell types, such as lymphocytes and phagocytes. Activation of C4 by the proteolytic enzyme, C1s, releases the C4a peptide from the α-chain, inducing a major conformational alteration of the C4b fragment that exposes or catalyzes a transacylation reaction involving an internal thiolester in the α-polypeptide. Attachment of C3b after activation of C3 by C3 convertases of either pathway occurs by the same mechanism: proteolytic release of the C3a peptide from the α-polypeptide of C3, causing a major conformational change in the C3b fragment that activates the thiol ester and induces transacylation to —OH groups. The second phase of recognition by complement is the binding of complexes containing covalently bound fragments of C3 and C4 by cells having receptors specific for these fragments. This chapter explains the structure/function relationships of CR1 and CR2 and presents a novel approach to antiinflammatory therapy that employs a recombinant soluble form of CR1. It also discusses the relationship between the natural ligand-binding site in CR2 to the binding site for the Epstein–Barr virus." @default.
- W54997757 created "2016-06-24" @default.
- W54997757 creator A5062651074 @default.
- W54997757 creator A5081907973 @default.
- W54997757 creator A5085595853 @default.
- W54997757 date "1990-01-01" @default.
- W54997757 modified "2023-09-24" @default.
- W54997757 title "CR1 and CR2: Receptors Mediating Cellular Recognition in the Complement System" @default.
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