2FIC

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

2FIC の概要

• エントリーDOI: 10.2210/pdb2fic/pdb
• 分子名称: Myc box-dependent-interacting protein 1, XENON (3 entities in total)
• 機能のキーワード: bar domain, homodimer, coiled-coils, endocytosis/exocytosis, membrane protein complex, endocytosis-exocytosis, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57789.77

構造登録者

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. (登録日: 2005-12-29, 公開日: 2006-11-14, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.99 Å)