Fig. 2: Dummy-containing Fc heterodimers with CH3 interface mutations that drive exchange reactions. | Nature Communications

Fig. 2: Dummy-containing Fc heterodimers with CH3 interface mutations that drive exchange reactions.

From: Format chain exchange (FORCE) for high-throughput generation of bispecific antibodies in combinatorial binder-format matrices

Fig. 2

CH3 interface mutations that drive the FORCE reaction were originally designed by modifying the existing 5HY9 structure. After successful generation of dummy Fc containing heterodimers, crystals and structures were generated from those Fcs. Shown here are these structures which confirmed the correctness of our initial modeling. a 5HY9 structure36 is characterized by the KiH mutations in ball and stick, an additional DS 354–349, and the salt bridge K370 and E357; b crystal structure of the KiH without DS25,35; the structures C, D, and F were generated as part of this work and are deposited in PDB ID’s 6YTB, 6YT7, and 6YSC. c Fc heterodimer with knob-dummy (6YT7); d structure of the Fc heterodimer with hole-dummy (6YSC); e structure of the interchain disulfide stabilized KiH Fc heterodimer of bsAb products36. f Structure of the KiH dummy dimer (6YBT).

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