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Molecular dynamic study of TMPA mediated dissociation of Nur77-LKB1 complex

Publication date:

Available online 30 June 2018

Source:Computational Biology and Chemistry

Author(s): Ikrormi Rungsung, Muthukumaran Rajagopalan, Amutha Ramaswamy

LKB1 protein is involved in the regulation of cell polarity by phosphorylating the AMPK under energetic stress conditions. LKB1 protein is expressed in both cytoplasm and nucleus. In the nucleus, LKB1 interacts with orphan nuclear receptor protein Nur77. It is reported that the interaction of LKB1 with Nur77 is disrupted by the small molecular ligand TMPA (ethyl 2-[2,3,4-trimethoxy-6-(1-octanoyl)phenyl]acetate), such that the LKB1 is enabled to play its role in cytoplasm and further to regulate/reduce the blood glucose level. In the present study, atomistic molecular dynamics simulations are performed to understand the dissociation mechanism of Nur77-LKB1 complex. The present study reveals that TMPAs induce an open-close motion of Nur77 which further decrease the stability of Nur77-LKB1 complex. As a consequence, the interface region in LKB1-Nur77 complex is more exposed for solvation and further releases the interactions existing between Nur77 and LKB1. Altogether, this study explains the TMPAs mediated Nur77-LKB1 complex dissociation.
Graphical abstract

Autoren:   Author(s): Ikrormi Rungsung, Muthukumaran Rajagopalan, Amutha Ramaswamy
Journal:   Computational Biology and Chemistry
Jahrgang:   2018
Erscheinungsdatum:   01.07.2018
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