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Article

Membrane binding by the endophilin N-BAR domain.

Biophysical journal - 18 Nov 2009

Cui Haosheng, Ayton Gary S, Voth Gregory A

Abstract excerpt

The structure of the endophilin N-terminal amphipathic helix Bin/Amphiphysin/Rvs-homology (N-BAR) domain is unique because of an additional insert helix under the arch of the N-BAR dimer. The structure of this additional helix has not been fully resolved in crystallographic studies, and thus presents a challenge to molecular-level analysis. Large-scale molecular-dynamics simulations were therefore employed to...

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Share to Protein Conformation
Share to Molecular Dynamics Simulation
Share to Adaptor Proteins, Signal Transducing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19917228
DOI: 10.1016/j.bpj.2009.08.043
PMCID: PMC2776271

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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