In Silico Investigation on KAR Signaling Reveals the Significant Dynamic Change of Its Receptor’s Structure

• Published in: Journal of chemical information and modeling 2022-04, Vol.62 (8), p.1933-1941
• Main Authors: Liu, Xiaoting, Zhang, Jilong
• Format: Article
• Language: English
• Subjects: Angiosperms; Binding; Carrier Proteins - metabolism; Catalytic Domain; Computational Biochemistry; Growth regulators; Ligands; Molecular dynamics; Plant Growth Regulators - metabolism; Receptors; Segments; Signal Transduction; Signaling
• ISSN: 1549-9596; 1549-960X
• DOI: 10.1021/acs.jcim.2c00004

Karrikins (KARs) have been identified as a class of smoke-derived plant growth regulators widely functioning among angiosperms. However, little is known about the mechanism by which these molecules trigger the relevant signal transduction. In this research, conventional molecular dynamics simulations were used to investigate the dynamical behavior of the apo- and holo-forms of the KAR receptor KAI2. The results show that the dynamic binding conformation of KAR1 in the active site is not completely consistent with that in the static crystal and is largely affected by the residue segment of the receptor, Tyr150–Asn180. The binding of the ligand with KAI2 changes the distribution of the electrostatic potential near the active site and drives the conformational transition of the Tyr150–Asn180 segment with strong internal positive correlation. A “dual induction” signaling mechanism is proposed in view of the present calculations. Our work paves way for in-depth understanding of the KAR signal transduction mechanism and sheds light on further experimental and theoretical exploration.