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.
Authors
- Alexander von Appen (ORCID: https://orcid.org/0000-0001-6528-2123)
- Aswin V. Muthachikavil (ORCID: https://orcid.org/0000-0001-7960-3565)
- Thomas D. Kühne (ORCID: https://orcid.org/0000-0001-5471-2407)
Institutions
- 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)
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
- 0.00