Immunology and Biotherapies

Molecular basis for antagonistic activity of anifrolumab, an anti-interferon–α receptor 1 antibody View full textDownload full textOpen accessDOI:10.1080/19420862.2015.1007810Li Penga, Vaheh Oganesyana, Herren Wua, William F Dall’Acquaa& Melissa M Damschrodera*

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Publishing models and article dates explainedReceived: 16 Oct 2014Accepted: 18 Nov 2014Accepted author version posted online: 21 Jan 2015Article Views: 84 Keywordsanifrolumab, MEDI546, IFNAR1, systemic sclerosis, epitope mapping, mutagenesis, enzymatic fragmentation, phage-peptide display, protein docking, Å, ångström, APBS, Adaptive Poisson-Boltzmann Solver, BSA, bovine serum albumin, CDR, complementarity-determining region, CHARMm, Chemistry at HARvard Macromolecular Mechanics, CHO, Chinese hamster ovary, EDTA, ethylene diamine tetra-acetic acid, ELISA, enzyme-linked immunosorbant assay, Fab, fragment antigen-binding, FBS, fetal bovine serum, Fc, fragment crystallizable, IFN, interferon, IFNAR1, interferon alpha receptor 1, IFNAR2, interferon alpha receptor 2, IgG, immunoglobulin, KD, equilibrium dissociation constant, kDa, kilodaltons,L-Cys, L-cysteine, MEMα, minimum essential alpha, MLE, murine lung epithelial, PBS, phosphate buffered saline, PBST, phosphate buffered saline tablets, PCR, polymerase chain reaction, PDB, protein data bank, Ph.D., phage display, PVDF, polyvinylidene difluoride, PyMOL, python-enhanced molecular graphics tool, RDOCK, rigid-body docking algorithm, RU, resonance units, SDS–PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis, SPR, surface plasmon resonance, VH, variable heavy, VL, variable light, ZDOCK, rigid-body docking algorithm