Ontology highlight
ABSTRACT:
SUBMITTER: Masuda M
PROVIDER: S-EPMC1500852 | biostudies-literature | 2006 Jun
REPOSITORIES: biostudies-literature
Masuda Michitaka M Takeda Soichi S Sone Manami M Ohki Takashi T Mori Hidezo H Kamioka Yuji Y Mochizuki Naoki N
The EMBO journal 20060608 12
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 doma ...[more]