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  • Title: Competition for binding sites on C3b by CR1, CR2, MCP, factor B and factor H.
    Author: Farries TC, Seya T, Harrison RA, Atkinson JP.
    Journal: Complement Inflamm; 1990; 7(1):30-41. PubMed ID: 2138950.
    Abstract:
    The reaction of radiolabeled C3b-binding proteins with C3b-coated particles has been investigated. CR1 binding was inhibited by factor H and factor B (in the presence of properdin), but not by properdin alone. CR2 and MCP binding were also inhibited by factor H. Therefore factor H, factor B, CR1, CR2 and MCP probably comprise a group of mutually competitive proteins with similar or overlapping binding sites on C3b. These results correlate with their structural homology and suggest that they all evolved from a single C3b-binding molecule. Factor H, CR1 and MCP are also cofactors for the factor-I-mediated cleavage of C3b. A species incompatibility between rat factor I and human CR1 for the cleavage of human C3b suggests the possibility that cofactors may also function by interacting directly with factor I.
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