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Xie, Bin; Maker, Allison; Priest, Andrew V; Dranow, David M; Phan, Jenny N; Edwards, Thomas E; Staker, Bart L; Myler, Peter J; Gumbiner, Barry M; Sivasankar, Sanjeevi
Proceedings of the National Academy of Sciences - PNAS, 08/2022, Volume: 119, Issue: 32Journal Article
E-cadherin (Ecad) is an essential cell-cell adhesion protein with tumor suppression properties. The adhesive state of Ecad can be modified by the monoclonal antibody 19A11, which has potential applications in reducing cancer metastasis. Using X-ray crystallography, we determine the structure of 19A11 Fab bound to Ecad and show that the antibody binds to the first extracellular domain of Ecad near its primary adhesive motif: the strand-swap dimer interface. Molecular dynamics simulations and single-molecule atomic force microscopy demonstrate that 19A11 interacts with Ecad in two distinct modes: one that strengthens the strand-swap dimer and one that does not alter adhesion. We show that adhesion is strengthened by the formation of a salt bridge between 19A11 and Ecad, which in turn stabilizes the swapped β-strand and its complementary binding pocket. Our results identify mechanistic principles for engineering antibodies to enhance Ecad adhesion.
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