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• W2586428163 abstract "Complement, a part of the humoral innate immune system, is divided into three pathways. The classical and mannose-binding lectin pathways are triggered by specific recognition of foreign targets. Conversely, the alternative pathway (AP) is actively down-regulated on host tissue. Glycosaminoglycans (GAGs) and sialylated glycans mediate host recognition of the AP as self-associated molecular patterns (SAMPs) to the regulatory protein factor H (FH). This review summarizes the more recent years of research on SAMP recognition by FH from a structural biology point of view and discusses implications for two complement-associated conditions, age-related macular degeneration (AMD) and atypical hemolytic uremic syndrome (aHUS). Taking into account crystal structures that elucidated FH binding to a bacterial evasion protein and to the thioester domain of C3b, the target of FH-mediated AP restriction, a novel atomistic model for the mechanism by which FH prevents AP activation on self surfaces is proposed." @default.
• W2586428163 created "2017-02-17" @default.
• W2586428163 creator A5016198415 @default.
• W2586428163 date "2017-06-01" @default.
• W2586428163 modified "2023-10-12" @default.
• W2586428163 title "The lectin self of complement factor H" @default.
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• W2586428163 doi "https://doi.org/10.1016/j.sbi.2017.01.005" @default.
• W2586428163 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28189794" @default.
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