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Article

Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy.

Nature communications - 21 Jul 2026

Noureddine Maya, Mikolajek Halina, Cowieson Nathan, Pinotsis Nikos, Robinson Paul, Slater Alexandre, Redwood Charles, Loughna Siobhan, Denning Chris, Mohammed Fiyaz, Gehmlich Katja

Abstract excerpt

Hypertrophic cardiomyopathy (HCM) is a genetic disease associated with sudden cardiac death. Variants in alpha-actinin-2 (ACTN2), a Z-disc protein that anchors actin thin filaments have been implicated in HCM, yet their structural consequences remain poorly defined. Here, we characterise seventeen HCM-associated ACTN2 variants spanning multiple domains using an integrated and tiered workflow combining...

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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: 42481460
DOI: 10.1038/s41467-026-75392-z
PMCID: PMC13388997

Genes

ACTN2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy.PMID 42481460Read ↗

Hypertrophic cardiomyopathy mutations in the calponin-homology domain of ACTN2 affect actin binding and cardiomyocyte Z-disc incorporation.Semantic proximity Read ↗

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Cardiomyopathy-Associated Variants Alter the Structure and Function of the α-Actinin-2 Actin-Binding DomainSemantic proximity Read ↗

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