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Article

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

The EMBO journal - 21 Jun 2006

Masuda Michitaka, Takeda Soichi, Sone Manami, Ohki Takashi, Mori Hidezo, Kamioka Yuji, Mochizuki Naoki

Abstract excerpt

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...

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Identifiers

PMID: 16763557
DOI: 10.1038/sj.emboj.7601176
PMCID: PMC1500852

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16763557-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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