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. 2023 Jul 6;14:1228962. doi: 10.3389/fphar.2023.1228962

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Copyright © 2023 Deng, Wang, Zhao, Tao, Zhang, Yang and Lei.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Three-dimensional (3D) structure diagram of the complex of Hu5F9-G4 and CD47 showed that Hu5F9-G4 had competitive antagonism with SIRPα. The orange and green peptide chains are the heavy chain and light chain of Hu5F9-G4, respectively. The light chain variable region peptide is represented in pink. The yellow peptide chain represents CD47, while the red peptide chain represents SIRPα. (A) Three-dimensional structure of CD47-ECD and Hu5F9-G4 complex after crystallization (PDB 5IWL). All complementary determiners of Hu5F9-G4 heavy chain and light chain variable CDR1 and CDR2 rings help Hu5F9-G4 bind CD47-ECD epitopes. (B) Hu5F9-G4 and SIRPα share binding pockets, which can be observed by superposition of Hu5F9-G4/CD47-ECD and SIRPα/CD47-ECD structures (PDB ID 2JJS).