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Article

Structures of the HER2-HER3-NRG1β complex reveal a dynamic dimer interface.

Nature - 1 Dec 2021

Diwanji Devan, Trenker Raphael, Thaker Tarjani M, Wang Feng, Agard David A, Verba Kliment A, Jura Natalia

Abstract excerpt

Human epidermal growth factor receptor 2 (HER2) and HER3 form a potent pro-oncogenic heterocomplex1-3 upon binding of growth factor neuregulin-1β (NRG1β). The mechanism by which HER2 and HER3 interact remains unknown in the absence of any structures of the complex. Here we isolated the NRG1β-bound near full-length HER2-HER3 dimer and, using cryo-electron microscopy, reconstructed the extracellulardomain module,...

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Share to Allosteric Regulation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Immunoglobulin Fab Fragments

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Share to Receptor, ErbB-2

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Source

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Identifiers

PMID: 34759323
DOI: 10.1038/s41586-021-04084-z
PMCID: PMC9298180

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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