Figure 1.
SR604 significantly improved binding affinity toward APC. (A) The sequence alignment of variable regions of HAPC1573, Humab-14, and SR604. CDRs are annotated using the Kabat numbering scheme. (B) Biacore sensorgrams (top) showing the association and dissociation curves of Humab-14 (left) and SR604 (right) binding to APC at different concentrations. The calculated affinity parameters are listed in the table at the bottom. (C) Model of APC-Humab-14 Fab complex computation simulated via the Protein-Protein Docking Module of BioLuminate. (D) Model of APC-SR604 Fab complex. (E-F) Protein-protein interactions between Humab-14 Fab (E) or SR604 Fab (F) and APC were calculated using the Protein Interaction Analysis module from BioLuminate (Schrödinger). The ribbon and surface maps were illustrated using Pymol (Schrödinger). RU, relative unit.

SR604 significantly improved binding affinity toward APC. (A) The sequence alignment of variable regions of HAPC1573, Humab-14, and SR604. CDRs are annotated using the Kabat numbering scheme. (B) Biacore sensorgrams (top) showing the association and dissociation curves of Humab-14 (left) and SR604 (right) binding to APC at different concentrations. The calculated affinity parameters are listed in the table at the bottom. (C) Model of APC-Humab-14 Fab complex computation simulated via the Protein-Protein Docking Module of BioLuminate. (D) Model of APC-SR604 Fab complex. (E-F) Protein-protein interactions between Humab-14 Fab (E) or SR604 Fab (F) and APC were calculated using the Protein Interaction Analysis module from BioLuminate (Schrödinger). The ribbon and surface maps were illustrated using Pymol (Schrödinger). RU, relative unit.

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