title: The crystal structure of the BAR domain from human Bin1/amphiphysin II and its implications for molecular recognition.
abstract: BAR domains are found in proteins that bind and remodel membranes and participate in cytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 A resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR domain are built upon "knobs-into-holes" packing of side chains, like those found in conventional left-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concave face. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein-protein interactions on the convex face of the dimer. Comparative analysis of structural features reveals that at least three architectural subtypes of the BAR domain are encoded in the human genome, represented by the Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. We discuss how these principal groups may differ in their potential to form regulatory heterotypic interactions.
authors.affiliation: Department of Biochemistry, University of Cambridge, UK.
authors.forename: Eva
authors.initials: E
authors.lastname: Casal
authors.forename: Luca
authors.initials: L
authors.lastname: Federici
authors.forename: Wei
authors.initials: W
authors.lastname: Zhang
authors.forename: Juan
authors.initials: J
authors.lastname: Fernandez-Recio
authors.forename: Eva-Maria
authors.initials: EM
authors.lastname: Priego
authors.forename: Ricardo Nuñez
authors.initials: RN
authors.lastname: Miguel
authors.forename: James B
authors.initials: JB
authors.lastname: DuHadaway
authors.forename: George C
authors.initials: GC
authors.lastname: Prendergast
authors.forename: Ben F
authors.initials: BF
authors.lastname: Luisi
authors.forename: Ernest D
authors.initials: ED
authors.lastname: Laue
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D006801:Humans; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein; D025521:Tumor Suppressor Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C101410:BIN1 protein, human; D009687:Nuclear Proteins; D025521:Tumor Suppressor Proteins