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Article

Bcl-2 and Bax interact via the BH1-3 groove-BH3 motif interface and a novel interface involving the BH4 motif.

The Journal of biological chemistry - 10 Sept 2010

Ding Jingzhen, Zhang Zhi, Roberts G Jane, Falcone Mina, Miao Yiwei, Shao Yuanlong, Zhang Xuejun C, Andrews David W, Lin Jialing

Abstract excerpt

The interaction of Bcl-2 family proteins at the mitochondrial outer membrane controls membrane permeability and thereby the apoptotic program. The anti-apoptotic protein Bcl-2 binds to the pro-apoptotic protein Bax to prevent Bax homo-oligomerization required for membrane permeabilization. Here, we used site-specific photocross-linking to map the surfaces of Bax and Bcl-2 that interact in the hetero-complex...

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Share to Amino Acid Motifs
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 20584903
DOI: 10.1074/jbc.M110.148361
PMCID: PMC2937903

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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