Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.

@article{Masuda2006EndophilinBD,
  title={Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.},
  author={Michitaka Masuda and Soichi Takeda and Manami Sone and Takashi Ohki and Hidezo Mori and Yuji Kamioka and Naoki Mochizuki},
  journal={The EMBO journal},
  year={2006},
  volume={25 12},
  pages={2889-97}
}
The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 A, has a unique structure consisting of a pair of helix-loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR… CONTINUE READING
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