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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Löw C,Weininger U,Lee H,Schweimer K,Neundorf I,Beck-Sickinger AG,Pastor RW,Balbach Jdoi
10.1529/biophysj.108.134155subject
Has Abstractpub_date
2008-11-01 00:00:00pages
4315-23issue
9eissn
0006-3495issn
1542-0086pii
S0006-3495(08)78570-9journal_volume
95pub_type
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