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1.  Dimer asymmetry defines α-catenin interactions  The F-actin
binding cytoskeletal protein α-catenin interacts with β-catenin-
cadherin complexes and stabilizes cell-cell junctions. The
β-catenin–α-catenin complex cannot bind to F-actin, whereas
interactions of α-catenin with the cytoskeletal protein vinculin
appear necessary to stabilize adherens junctions. Here we report
the crystal structure of nearly full-length human α-catenin at
3.7 Å resolution. α-Catenin forms an asymmetric dimer, where the
four-helix bundle domains of each subunit engage in distinct
intermolecular interactions. This results in a left handshake-
like dimer, where the two subunits have remarkably different
conformations. The crystal structure explains why dimeric
α-catenin has a higher affinity for F-actin than monomeric
α-catenin, why the β-catenin–α-catenin complex does not bind to
F-actin, how activated vincu