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Fig. 2 | Journal of Hematology & Oncology

Fig. 2

From: A pH-dependent anti-CD47 antibody that selectively targets solid tumors and improves therapeutic efficacy and safety

Fig. 2

Structural characterization of the pH-dependent binding of BC31M4. a Crystal structure of the BC31M5-CD47 complex, depicted as ribbons. T108 (orange) in VH and histidines (red) in VL are shown as sticks. b Detailed view of the BC31M5-CD47 interface. Gray dashed lines indicate electrostatic interactions between BC31M5 and CD47. Side chains of contacted residues are shown as sticks. Yellow dashed lines indicate π-contacts. c The three histidines (H38, H55, or H107) in the VL of BC31M4 (in phage-scFv form) were mutated into any other amino acids individually (site saturation mutagenesis). These mutants binding to CD47 at pH7.4 and pH 6.5 were measured by ELISA. d Serial dilutions of BC31M4 mutants (in hIgG1 form) with the indicated double or triple histidine-to-arginine substitutions binding to CD47-ECD at pH7.4 and pH 6.8, measured by ELISA

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