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Updated: Feb 8, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
Published on: March 14, 2019
Molecular dynamics study of TMPA mediated dissociation of Nur77-LKB1 complex
Ikrormi Rungsung1, Muthukumaran Rajagopalan1, Amutha Ramaswamy1
1Centre for Bioinformatics, School of Life Sciences, Pondicherry University, Puducherry, 605014, India.
Abstract:
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.
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