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• W2770657816 abstract "Abstract This chapter provides an overview of the state of knowledge of the set of five complement factor H-related proteins (CFHRs) in humans. A brief description is included of their physicochemical properties, structures, binding partners and potential roles as modulators of complement regulation. Their genomic organisation is outlined and some important disease-related polymorphisms, many involving genomic rearrangements, are summarised. Like complement factor H (CFH), CFHRs are composed exclusively from complement control protein (CCP) modules (also known as SCRs or sushi domains). Group I CFHRs, comprising CFHRs 1, 2 and 5, possess dimerisation motifs in their N-terminal CCP modules. Group II CFHRs, comprising CFHRs 3 and 4 lack this motif. Group I CFHR proteins form homodimers and heterodimers. While CFHRs were reported to have weak complement regulatory activity, most if not all of the CFHRs can compete with CFH for binding to C3b, iC3b, C3d(g), various self-surface markers and several microbial proteins; hence, they can act as deregulators of complement activation." @default.
• W2770657816 created "2017-12-04" @default.
• W2770657816 creator A5028477285 @default.
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• W2770657816 date "2018-01-01" @default.
• W2770657816 modified "2023-09-26" @default.
• W2770657816 title "Factor H-Related Proteins 1–5" @default.
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• W2770657816 doi "https://doi.org/10.1016/b978-0-12-810420-0.00031-6" @default.
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