1URU

Amphiphysin BAR domain from Drosophila

1URU の概要

• エントリーDOI: 10.2210/pdb1uru/pdb
• 分子名称: AMPHIPHYSIN (2 entities in total)
• 機能のキーワード: endocytosis, coiled-coil, membrane curvature
• 由来する生物種: DROSOPHILA MELANOGASTER (FRUIT FLY)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28269.15

構造登録者

Evans, P.R.,Kent, H.M. (登録日: 2003-11-06, 公開日: 2003-12-04, 最終更新日: 2024-11-20)

主引用文献

Peter, B.J.,Kent, H.M.,Mills, I.G.,Vallis, Y.,Butler, J.G.,Evans, P.R.,Mcmahon, H.T.
Bar Domains as Sensors of Membrane Curvature: The Amphiphysin Bar Structure
Science, 303:495-, 2004

PubMed Abstract: 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 find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.

PubMed: 14645856
DOI: 10.1126/SCIENCE.1092586

実験手法

X-RAY DIFFRACTION (2.6 Å)