2RMY

Structure of the N-terminal BARpeptide in SDS micelles

2RMY の概要

• エントリーDOI: 10.2210/pdb2rmy/pdb
• NMR情報: BMRB: 11050
• 分子名称: Myc box-dependent-interacting protein 1 (1 entity in total)
• 機能のキーワード: barpeptide, micelle, nmr-structure, alternative splicing, anti-oncogene, cell cycle, coiled coil, cytoplasm, developmental protein, differentiation, endocytosis, host-virus interaction, nucleus, phosphoprotein, sh3 domain
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform BIN1: Nucleus. Isoform IIA: Cytoplasm: O00499
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3714.42

構造登録者

Loew, C.,Weininger, U.,Balbach, J. (登録日: 2007-12-03, 公開日: 2008-10-14, 最終更新日: 2024-05-29)

主引用文献

Low, C.,Weininger, U.,Lee, H.,Schweimer, K.,Neundorf, I.,Beck-Sickinger, A.G.,Pastor, R.W.,Balbach, J.
Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers
Biophys.J., 95:4315-4323, 2008

PubMed Abstract: Bin/Amphiphysin/Rvs-homology (BAR) domains generate and sense membrane curvature by binding the negatively charged membrane to their positively charged concave surfaces. N-BAR domains contain an N-terminal extension (helix-0) predicted to form an amphipathic helix upon membrane binding. We determined the NMR structure and nano-to-picosecond dynamics of helix-0 of the human Bin1/Amphiphysin II BAR domain in sodium dodecyl sulfate and dodecylphosphocholine micelles. Molecular dynamics simulations of this 34-amino acid peptide revealed electrostatic and hydrophobic interactions with the detergent molecules that induce helical structure formation from residues 8-10 toward the C-terminus. The orientation in the micelles was experimentally confirmed by backbone amide proton exchange. The simulation and the experiment indicated that the N-terminal region is disordered, and the peptide curves to adopted the micelle shape. Deletion of helix-0 reduced tubulation of liposomes by the BAR domain, whereas the helix-0 peptide itself was fusogenic. These findings support models for membrane curving by BAR domains in which helix-0 increases the binding affinity to the membrane and enhances curvature generation.

PubMed: 18658220
DOI: 10.1529/biophysj.108.134155

実験手法

SOLUTION NMR