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• W2610804734 abstract "Neuromyelitis optica (NMO) is an inflammatory demyelinating disease of the central nervous system in which most patients have serum autoantibodies (called NMO-IgG) that bind to astrocyte water channel aquaporin-4 (AQP4). A potential therapeutic strategy in NMO is to block the interaction of NMO-IgG with AQP4. Building on recent observation that some single-point and compound mutations of the AQP4 extracellular loop C prevent NMO-IgG binding, we carried out comparative Molecular Dynamics (MD) investigations on three AQP4 mutants, TP137-138AA, N153Q and V150G, whose 295-ns long trajectories were compared to that of wild type human AQP4. A robust conclusion of our modeling is that loop C mutations affect the conformation of neighboring extracellular loop A, thereby interfering with NMO-IgG binding. Analysis of individual mutations suggested specific hydrogen bonding and other molecular interactions involved in AQP4-IgG binding to AQP4." @default.
• W2610804734 created "2017-05-12" @default.
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• W2610804734 date "2017-08-01" @default.
• W2610804734 modified "2023-10-17" @default.
• W2610804734 title "Comparative molecular dynamics study of neuromyelitis optica-immunoglobulin G binding to aquaporin-4 extracellular domains" @default.
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• W2610804734 doi "https://doi.org/10.1016/j.bbamem.2017.05.001" @default.
• W2610804734 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5581535" @default.
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