BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure

@article{Peter2004BARDA,
  title={BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure},
  author={Brian Jon Peter and Helen M. Kent and Ian G. Mills and Yvonne Vallis and Peter J Butler and Philip R. Evans and Harvey T. McMahon},
  journal={Science},
  year={2004},
  volume={303},
  pages={495 - 499}
}
The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we… 

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

The crystal structure of the BAR domain from the human Bin1 protein at 2.0 A resolution is reported and calculations indicate that the Bin1BAR domain contains two potential sites for protein-protein interactions on the convex face of the dimer.

Amphipathic motifs in BAR domains are essential for membrane curvature sensing

BAR (Bin/Amphiphysin/Rvs) domains and amphipathic α‐helices (AHs) are believed to be sensors of membrane curvature thus facilitating the assembly of protein complexes on curved membranes. Here, we

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

It is proposed that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino‐terminal amphipathic helix.

Structural insights into the cooperative remodeling of membranes by amphiphysin/BIN1

This study indicates that the H0 helix and the BAR tip are necessary for efficient and organized self-assembly of amphiphysin/N-BAR.
...

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