Molecular Dynamics Simulations Reveal Structural Interconnections within Sec14-PH Bipartite Domain from Human Neurofibromin
Abstract
:1. Introduction
2. Results
2.1. PH Portion of Sec14-PH Domain Is Independently Stable and Shows Scarce Flexibility
2.2. Dynamic Behaviour of the Whole Wild-Type Sec14-PH Domain
2.3. The K1750Δ Mutation Weakens the Interconnection between the Two Portions of the Bipartite Sec14-PH Domain
2.4. Opening of the Lipid Pocket
3. Discussion
4. Materials and Methods
4.1. Systems Setup
4.2. Molecular Dynamics Simulations and Analysis
Supplementary Materials
Author Contributions
Funding
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Rizza, F.; Vertemara, J.; Tisi, R. Molecular Dynamics Simulations Reveal Structural Interconnections within Sec14-PH Bipartite Domain from Human Neurofibromin. Int. J. Mol. Sci. 2022, 23, 5707. https://doi.org/10.3390/ijms23105707
Rizza F, Vertemara J, Tisi R. Molecular Dynamics Simulations Reveal Structural Interconnections within Sec14-PH Bipartite Domain from Human Neurofibromin. International Journal of Molecular Sciences. 2022; 23(10):5707. https://doi.org/10.3390/ijms23105707
Chicago/Turabian StyleRizza, Fabio, Jacopo Vertemara, and Renata Tisi. 2022. "Molecular Dynamics Simulations Reveal Structural Interconnections within Sec14-PH Bipartite Domain from Human Neurofibromin" International Journal of Molecular Sciences 23, no. 10: 5707. https://doi.org/10.3390/ijms23105707