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Significance Antibodies binding to their cognate cellular receptors can trigger important downstream immune responses. We mapped out critical amino acids on the IgA1 antibody that govern binding to its specific receptor, FcαRI. We found that two of the most important amino acids were located on a different IgA1 domain than the rest of the binding site, separated by a flexible linker. To better understand the interplay between receptor binding and dynamic motions in IgA1, we conducted dynamics simulations on the system. The results indicate that receptor binding perturbs IgA1 conformational dynamics over long distances and can link the receptor binding site to the hinge region of IgA1. We validate this finding experimentally, which has implications for the kidney disease IgA nephropathy.

proceedings of the national academy of sciences of the united states of america

FcαRI binding at the IgA1 C <sub>H</sub> 2–C <sub>H</sub> 3 interface induces long-range conformational changes that are transmitted to the hinge region

FcαRI binding at the IgA1 C H 2–C H 3 interface induces long-range conformational changes that are transmitted to the hinge region

FcαRI binding at the IgA1 C _H 2–C _H 3 interface induces long-range conformational changes that are transmitted to the hinge region