Novel Electrostatic Mechanisms Controlling the Conformational Switching of L-plastin
Date
2018-06-12
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Abstract
L-plastin is an actin-bundling protein that promotes the motility of both hematopoietic and metastatic cancer cells. The high definition structure of the calcium-binding regulatory domain of human L-plastin was recently determined, allowing computational research on this portion of the protein. The Drude polarizable force field was used to provide accurate computational simulations of the calcium-binding domain in conjunction with experimental validation to shown that L-plastin can regulate calcium-binding, and thus actin-bundling, through internal electrostatic interactions. Through this work the Drude force field was also benchmarked, to show that it provides comparable results to classical force fields with the added ability to simulate polarizability. Overall, a novel mechanism which allows L-plastin to self-regulate its calcium-binding affinity was developed.
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Keywords
L-plastin, Protein conformational dynamics, MD Simulation, Calcium-binding regulation, Polarizable force field
Citation
Fanning, J. K. (2018). Novel Electrostatic Mechanisms Controlling the Conformational Switching of L-plastin (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/32009