Computational Characterization of the Role of <scp>LEM2</scp> / <scp>LaminA</scp> Interactions on the Stability of <scp>BAF</scp> ‐Dimer Using Molecular Simulations

The effect of the presence of the BAF-binding LEM-domain and LaminA Ig-fold on the stability of the BAF dimer was studied qualitatively using non-equilibrium pull simulations and quantitatively through the calculation of the potential of mean force profile along BAF-BAF separation distance. We find that hydrophobicity plays a significant role in stabilizing the BAF dimer when LEM-domain and LaminA are bound. The role of LEM-domain and LaminA in stabilizing the BAF dimer is explored by quantifying the strength of interaction between them, which are critical components of the nuclear lamina.

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Publication Details

Journal
Proteins Structure Function and Bioinformatics
Published
2025-12-18
DOI
https://doi.org/10.1002/prot.70105
Primary Topic
Nuclear Structure and Function
Type
article
Field-Weighted Citation Impact
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article

Computational Characterization of the Role of LEM2 / LaminA Interactions on the Stability of BAF ‐Dimer Using Molecular Simulations

Alexander von Appen, Aswin V. Muthachikavil, Thomas D. Kühne
Proteins Structure Function and Bioinformatics
Nuclear Structure and Function
article

Computational Characterization of the Role of LEM2 / LaminA Interactions on the Stability of BAF ‐Dimer Using Molecular Simulations

Alexander von Appen, Aswin V. Muthachikavil, Thomas D. Kühne
article en

Abstract

The effect of the presence of the BAF-binding LEM-domain and LaminA Ig-fold on the stability of the BAF dimer was studied qualitatively using non-equilibrium pull simulations and quantitatively through the calculation of the potential of mean force profile along BAF-BAF separation distance. We find that hydrophobicity plays a significant role in stabilizing the BAF dimer when LEM-domain and LaminA are bound. The role of LEM-domain and LaminA in stabilizing the BAF dimer is explored by quantifying the strength of interaction between them, which are critical components of the nuclear lamina.

Proteins Structure Function and Bioinformatics
Helmholtz-Zentrum Dresden-Rossendorf (DE), Center for Advanced Systems Understanding (DE), Max Planck Institut für Zellbiologie (DE), Max Planck Institute of Molecular Cell Biology and Genetics (DE)
Openalex Percentile: Top 62%
Nuclear Structure and Function
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