2D4C

Crystal structure of the endophilin BAR domain mutant

2D4C の概要

• エントリーDOI: 10.2210/pdb2d4c/pdb
• 関連するPDBエントリー: 1X03 1X04
• 分子名称: SH3-containing GRB2-like protein 2, CALCIUM ION (3 entities in total)
• 機能のキーワード: bar domain, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q99962
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 116265.05

構造登録者

Masuda, M.,Takeda, S. (登録日: 2005-10-13, 公開日: 2006-07-11, 最終更新日: 2023-10-25)

主引用文献

Masuda, M.,Takeda, S.,Sone, M.,Ohki, T.,Mori, H.,Kamioka, Y.,Mochizuki, N.
Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
Embo J., 25:2889-2897, 2006

PubMed Abstract: 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 domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose 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.

PubMed: 16763557
DOI: 10.1038/sj.emboj.7601176

実験手法

X-RAY DIFFRACTION (2.4 Å)