Evidence map›Paper›PMID 41759735›Full record

ArticleThe Journal of biological chemistry2026

Stability and interaction defects in the Sin3A-PAH1 αα-hub domain associated with loss-of-function variants.

Amanda D Due, Sigrid Jørsboe, Louise T Jensen, Charlotte O'Shea, Majken Staulund, Martin Willemoës, Birthe B Kragelund, Ida M Z Sjøgaard, Karen Skriver

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Amanda D DueREPIN, University of Copenhagen, Copenhagen, Denmark; Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark; Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Sigrid JørsboeLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark.
Louise T JensenLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark.
Charlotte O'SheaLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark.
Majken StaulundLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark.
Martin WillemoësLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark.
Birthe B KragelundREPIN, University of Copenhagen, Copenhagen, Denmark; Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark; Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Ida M Z SjøgaardREPIN, University of Copenhagen, Copenhagen, Denmark; Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark. Electronic address: ida.zobbe@bio.ku.dk.
Karen SkriverREPIN, University of Copenhagen, Copenhagen, Denmark; Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark. Electronic address: kskriver@bio.ku.dk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hub proteins organize large interactomes using their hub domains for protein-protein interactions. αα-hub domains are present in transcriptional regulators, such as Switch-insensitive 3A (Sin3A), an integral scaffolding protein of histone deacetylation complexes. Here, we relate αα-hub stability to function by structural and thermodynamic studies of the Sin3A-paired amphipathic helix 1 (PAH1) wt hub domain and two predicted loss-of-function variants (A126V and K155E) found in patients with the neurodevelopmental Witteveen-Kolk syndrome. For an αα-hub domain, the PAH1 domain is relatively stable with a ΔG

Indexed as

Loss of Function MutationRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexHumansModels, MolecularProtein BindingProtein DomainsProtein StabilityThermodynamicsRepressor ProteinsSIN3A transcription factorSin3 Histone Deacetylase and Corepressor ComplexdiseaseIDPIDRprotein domainprotein foldingprotein–protein interactionside-chain variantstructure–functiontranscription coregulator

Identifiers

PMID41759735
PMCPMC13068551

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.