@article {389,
	title = {Direct Observation of Bin/amphiphysin/Rvs (BAR) Domain-induced Membrane Curvature by Means of Molecular Dynamics Simulations},
	journal = {Proc Natl Acad Sci U S A},
	volume = {103},
	number = {41},
	year = {2006},
	note = {Blood, Philip D Voth, Gregory A 1 S10RR17214-01/RR/NCRR NIH HHS/United States GM0637-96/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, U.S. Gov{\textquoteright}t, Non-P.H.S. United States Proceedings of the National Academy of Sciences of the United States of America Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15068-72. Epub 2006 Sep 28.},
	pages = {15068-72},
	abstract = {<p>The process of membrane curvature generation by BAR (Bin/amphiphysin/Rvs) domains is thought to involve the plastering of the negatively charged cell membrane to the positively charged concave surface of the BAR domain. Recent work [Peter, B. J., et al. (2004) Science, 303,495-499; Masuda, M., et al. (2006) EMBO J. 25, 2889-2897; and Gallop, J. L., et al. (2006) EMBO J. 25, 2898-2910] has demonstrated the importance of the charged, crescent-shaped surface and the N-terminal amphipathic helices (present in N-BAR domains) for generating membrane curvature. These experiments suggest that curvature is generated by the synergistic action of the N-terminal helices embedding in the lipid bilayer and the charged crescent-shaped dimer acting to "scaffold" membrane curvature. Here, we present atomistic molecular dynamics simulations that directly show membrane binding to the concave face of N-BAR domains, resulting in the generation of local membrane curvature that matches the curvature presented by the BAR domain. These simulations provide direct molecular-scale evidence that BAR domains create curvature by acting as a scaffold, forcing the membrane to locally adopt the intrinsic shape of the BAR domain. We find that BAR domains bind strongly through the maximum curvature surface and, additionally, at an orientation that presents a lesser degree of curvature, thus enabling N-BAR domains to induce a range of local curvatures. Finally, we find that the N-terminal region may play a role in biasing the orientations of N-BAR domains on the membrane surface to those that favor binding to the concave face and subsequent membrane bending.</p>},
	keywords = {Animals Cell Membrane/*chemistry/physiology *Computer Simulation Crystallography, Biological *Models, Molecular Nerve Tissue Proteins/*chemistry/physiology Protein Structure, Tertiary Static Electricity Thermodynamics Transcription Factors/*chemistry/physiology, X-Ray Cytoskeletal Proteins/*chemistry/physiology Drosophila Proteins/*chemistry/physiology Forkhead Transcription Factors Humans Lipid Bilayers/chemistry *Models},
	doi = {10.1073/pnas.0603917103},
	author = {Blood, P. D. and G. A. Voth}
}
