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• W2024742078 abstract "Infection-inflammation mediated interactions between human ficolin and the pathogen GlcNAc is associated with local acidosis, leading to antimicrobial action. Therefore, revealing the precise molecular conformation induced by pH-shift is crucial in understanding the immune response. Here, we performed constant-pH molecular dynamics simulations on the L-ficolin fibrinogen-like domain over pH 4.5–9. An unusual cis-Asn244-Cys245 peptide bond prevailed over the pH range in the S1 binding site. Analysis of the hydrogen-bond network at S1 suggested Asn244 to be indispensible for maintaining the cis form of Asn244-Cys245, and the absence of the hydroxyl group on Phe262 accounts for the lack of GlcNAc binding." @default.
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• W2024742078 date "2011-01-01" @default.
• W2024742078 modified "2023-09-25" @default.
• W2024742078 title "Peptide Isomerization Induced by pH Change Regulates the S1 Binding Site in Ficolins" @default.
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• W2024742078 doi "https://doi.org/10.1071/ch11050" @default.
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