Fig. 1: Functional and structural characterization of mAb1 and CCL1 binding to CCR8. | Nature Communications

Fig. 1: Functional and structural characterization of mAb1 and CCL1 binding to CCR8.

From: Structural basis of antibody inhibition and chemokine activation of the human CC chemokine receptor 8

Fig. 1

Analysis of mAb1 and CCL1 binding on CCR8 activation (a) and of mAb1 competition binding on CCL1-induced CCR8 activation (b) by Ca2+ influx cellular assay. Experiments were performed in duplicate, with error bars showing standard deviation. c Analysis of mAb1-mediated inhibition of CCL1-induced ERK phosphorylation, as analyzed by total ERK and phospho-ERK western blot as a function of mAb1 concentration. Data are representative of two independent experiments. d Cryo-EM map and model of the Fab1-CCR8 complex. e Cryo-EM map and model of CCL1-CCR8-Gi1-scFv16. Protein subunits in d and e are colored as follows: CCR8 inactive state, wheat; light chain (LC) of Fab1, pink; heavy chain (HC) of Fab1, green; CCR8 active state, teal; CCL1, magenta; GĪ±i1, blue; GĪ²1, green; GĪ³2, pink; scFv16, gray. Source data are provided as a Source Data file.

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