Abstract
Kinesin is a motor protein that delivers cargo inside a cell. Kinesin has many different families, but they perform basically same function and have same motions. The walking motion of kinesin enables the cargo delivery inside the cell. Autoinhibition of kinesin is important because it explains how function of kinesin inside a cell is stopped. Former researches showed that tail binding is related to autoinhibition of kinesin. In this work, we performed normal mode analysis with elastic network model using different conformation of kinesin to determine the effect of tail binding by considering four models such as functional form, autoinhibited form, autoinhibited form without tail, and autoinhibited form with carbon structure. Our calculation of the thermal fluctuation and cross-correlation shows the change of tail-binding region in structural motion. Also strain energy of kinesin showed that elimination of tail binding effect leads the structure to have energetically similar behavior with the functional form.
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Acknowledgments
S.N. gratefully acknowledges the financial support from Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and Future Planning (MSIP) (No. 2007-0056094) and (No. 2013-055175). H.J.C. is grateful to the financial support from Global Ph.D. Fellowship Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (No. 2014H1A2A1021042).
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Jae In Kim and Hyun Joon Chang have made equal contributions in this work.
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Kim, J.I., Chang, H.J. & Na, S. Identification of tail binding effect of kinesin-1 using an elastic network model. Biomech Model Mechanobiol 14, 1107–1117 (2015). https://doi.org/10.1007/s10237-015-0657-1
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DOI: https://doi.org/10.1007/s10237-015-0657-1