Fig. 6: Structure based mutagenesis studies identified an antagonistic mOSM mutant and key hOSMR residues involved in hOSM binding and signaling. | Nature Communications

Fig. 6: Structure based mutagenesis studies identified an antagonistic mOSM mutant and key hOSMR residues involved in hOSM binding and signaling.

From: Structures of complete extracellular assemblies of type I and type II Oncostatin M receptor complexes

Fig. 6: Structure based mutagenesis studies identified an antagonistic mOSM mutant and key hOSMR residues involved in hOSM binding and signaling.

a STAT3-luciferase reporter assay was performed in mouse NIH3T3 cells after treating the cells with short form mOSM WT and five mutant proteins with mutations at Site 3. The data shown are representative of 3 independent experiments with similar results. Error bars represent standard deviations. RLU: relative luminescence units. b WT hOSMR or six hOSMR mutants were stably overexpressed in human Ramos.2G6.4C10.stat3luc cells; STAT3-luciferase reporter assay was performed after treating the cells with E.coli-derived short form hOSM protein (R&D, #295-OM). The data shown are representative of 3 independent experiments with similar results. Error bars represent standard deviations. Source data are provided as a Source Data file.

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