2fic
From Proteopedia
The crystal structure of the BAR domain from human Bin1/Amphiphysin II and its implications for molecular recognition
Overview
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.
About this Structure
2FIC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of the BAR domain from human Bin1/amphiphysin II and its implications for molecular recognition., Casal E, Federici L, Zhang W, Fernandez-Recio J, Priego EM, Miguel RN, DuHadaway JB, Prendergast GC, Luisi BF, Laue ED, Biochemistry. 2006 Oct 31;45(43):12917-28. PMID:17059209 Page seeded by OCA on Sun May 4 03:55:55 2008
