Cadherins can dimerize via asymmetric interactions.

Cadherins are essential cell-cell adhesion proteins that interact in two distinct conformations: X-dimers and strand-swap dimers. Both X-dimers and strand-swap dimers are thought to exclusively rely on symmetric sets of interactions between key amino acids on both cadherin binding partners. Here, we use single-molecule atomic force microscopy and computer simulations to show that symmetry in cadherin binding is dispensable and that cadherins can also interact in a novel conformation that asymmetrically incorporates key elements of both strand-swap dimers and X-dimers. Our results clarify the biophysical rules for cadherin binding and demonstrate that cadherins interact in a more diverse range of conformations than previously understood. © 2022 Federation of European Biochemical Societies.

Citation

Andrew Vae Priest, Ramesh Koirala, Sanjeevi Sivasankar. Cadherins can dimerize via asymmetric interactions. FEBS letters. 2022 Jul;596(13):1639-1646

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PMID: 35532156

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