Interaction of Kinesin-5 Motor Domain with Tubulin Dimer
Abstract
Kinesin-5 in fission yeast also known as Cut7 is a molecular motor essential for separation of spindle fibers during the mitotic cell division. Kinesin-5 crosslinks the spindle microtubules and slides them towards the spindle poles. Molecular dynamics simulation was performed, and various analysis were carried out to study the interaction of kinesin-5 motor domain with alpha and beta tubulins. From electrostatic potential distribution, it is observed that binding interface of kinesin-5 motor domain is mainly positive and tubulin dimer is mainly negative, which shows the stronger interaction between them. Further when electric field lines were plotted, we observed more field lines at kinesin-5 motor and beta tubulin interface. Meaning the interaction of kinesin-5 with beta tubulin is stronger. Moreover, the binding energies, salt-bridges, hydrogen bonds, were analyzed in detail, which again supported the stronger interaction of kinesin-5 motor with beta tubulin. Furthermore, key residues at the binding interfaces of kinesin-5 motor domain and tubulin dimers were identified, which are believed to be useful for developing drug against cancerous cells.
Subject Area
Computational chemistry|Cellular biology|Biochemistry|Polymer chemistry
Recommended Citation
Karki, Chitra Bahadur, "Interaction of Kinesin-5 Motor Domain with Tubulin Dimer" (2021). ETD Collection for University of Texas, El Paso. AAI28716042.
https://scholarworks.utep.edu/dissertations/AAI28716042