2FIC

The crystal structure of the BAR domain from human Bin1/Amphiphysin II and its implications for molecular recognition

Summary for 2FIC

• Entry DOI: 10.2210/pdb2fic/pdb
• Descriptor: Myc box-dependent-interacting protein 1, XENON (3 entities in total)
• Functional Keywords: bar domain, homodimer, coiled-coils, endocytosis/exocytosis, membrane protein complex, endocytosis-exocytosis, membrane protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 57789.77

Authors

Casal, E.,Federici, L.,Zhang, W.,Fernandez-Recio, J.,Priego, E.M.,Miguel, R.N.,Duhadaway, J.B.,Prendergast, G.C.,Luisi, B.F.,Laue, E.D. (deposition date: 2005-12-29, release date: 2006-11-14, Last modification date: 2024-03-13)

Primary citation

Casal, E.,Federici, L.,Zhang, W.,Fernandez-Recio, J.,Priego, E.M.,Miguel, R.N.,Duhadaway, J.B.,Prendergast, G.C.,Luisi, B.F.,Laue, E.D.
The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition
Biochemistry, 45:12917-12928, 2006

PubMed 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.

PubMed: 17059209
DOI: 10.1021/bi060717k

Experimental method

X-RAY DIFFRACTION (1.99 Å)