Computational prediction and in vitro analysis of the potential ligand binding site within the extracellular ATP receptor, P2K2

ABSTRACT

The plant extracellular ATP (eATP) receptor, P2K2, binds eATP with strong ligand affinity through its extracellular lectin domain. Ligand binding activates the intracellular kinase domain of P2K2 resulting in a variety of intracellular responses and, ultimately, increased plant immunity to invading fungal and bacterial pathogens. Here, using a computational prediction approach, we developed a tertiary structure model of the P2K2 extracellular lectin domain. In silico target docking of ATP to the P2K2-binding site predicted interaction with several residues through hydrophobic interactions and hydrogen bonding. Our confirmation of the modeling was obtained by showing that H99, R144, and S256 are key residues essential for in vitro binding of ATP by P2K2.

KEYWORDS:

• Extracellular ATP
• P2K2
• purinoreceptor
• lectin receptor kinase
• in silico model

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

The research was supported by the National Institutes of National Institute of General Medical Sciences (grant no. R01GM121445), the Next-Generation BioGreen 21 Program Systems and Synthetic Agrobiotech Center, Rural Development Administration, PJ013254, PJ01116604 (grant nos. PJ013254 and PJ01116604), and the 3rd Call of the ERA-NET for Coordinating Action in Plant Sciences, with funding from the US National Science Foundation (grant no. 1826803).