Figure 1
From: Anti-leukemic activity and tolerability of anti-human CD47 monoclonal antibodies
C47B161, C47B222 and B6H12.2 Fabs have steric clashes with SIRPα. (a) Structural overlay of Fab/CD47 complexes onto the SIRPα/CD47 complex showing regions of clash between Fab and SIRPα. The overlay was achieved by superposition of equivalent CD47 Cα atoms in both complexes. The membrane-proximal C15G mutation that was introduced to prevent CD47 aggregation is shown as a yellow sphere. (b) Regions of overlap between each epitope and the SIRPα binding site (red areas). The structure of CD47 from the C47B222 complex was used in (b). (c) Epitope regions of C47B161, C47B222 and B6H12.2. The epitope residues are shaded and SIRPα binding residues are marked with a dot above the human CD47 ECD sequence. The secondary structure of CD47 is shown above the sequence with arrows and cylinders representing β-strands and helices, respectively.
