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Article

Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG.

Nature communications - 7 Feb 2012

Li Xiaohua, He Liqiang, Che Ka Hing, Funderburk Sarah F, Pan Lifeng, Pan Nina, Zhang Mingjie, Yue Zhenyu, Zhao Yanxiang

Abstract excerpt

Beclin 1 is a core component of the Class III Phosphatidylinositol 3-Kinase VPS34 complex. The coiled coil domain of Beclin 1 serves as an interaction platform for assembly of distinct Atg14L- and UVRAG-containing complexes to modulate VPS34 activity. Here we report the crystal structure of the coiled coil domain that forms an antiparallel dimer and is rendered metastable by a series of 'imperfect' a-d' pairings...

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Identifiers

PMID: 22314358
DOI: 10.1038/ncomms1648
PMCID: PMC3293417

Genes

UVRAG

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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