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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Stability and interaction defects in the Sin3A-PAH1 αα-hub domain associated with loss-of-function variants

Amanda D Due1, Sigrid Jørsboe2, Louise T Jensen2

  • 1REPIN, 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.

The Journal of Biological Chemistry
|February 27, 2026
PubMed
Summary

Hub proteins like Sin3A are crucial for cellular interactions. This study reveals how mutations in the Sin3A-PAH1 domain affect its stability and binding, impacting Witteveen-Kolk syndrome.

Keywords:
IDPIDRdiseaseprotein domainprotein foldingprotein–protein interactionside-chain variantstructure–functiontranscription coregulator

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