| Abstract
| - BAR domains are found in proteins that bind and remodel membranes and participate incytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from thehuman Bin1 protein at 2.0 Å resolution. Both the quaternary and tertiary architectures of the homodimericBin1BAR domain are built upon “knobs-into-holes” packing of side chains, like those found in conventionalleft-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concaveface. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein−proteininteractions on the convex face of the dimer. Comparative analysis of structural features reveals that atleast three architectural subtypes of the BAR domain are encoded in the human genome, represented bythe Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. We discuss how these principal groups maydiffer in their potential to form regulatory heterotypic interactions.
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