Computational prediction and in vitro analysis of the potential ligand binding site within the extracellular ATP receptor, P2K2. (31st December 2023)

• Record Type: Journal Article
• Authors: Cho, Sung-Hwan; Nguyen, Cuong the; Pham, an Quoc; Stacey, Gary
• Is Part Of: Plant signaling & behavior. Volume 18:Number 1(2023)
• Publication Date: 2023-12-31
• Subjects: Extracellular ATP -- P2K2 -- purinoreceptor -- lectin receptor kinase -- in silico model; Plant ecophysiology -- Periodicals; Plant cellular signal transduction -- Periodicals; Plant cellular signal transduction; Plant ecophysiology; Periodicals; Electronic journals; 581
• DOI: 10.1080/15592324.2023.2173146
• Languages: English
• ISSNs: 1559-2316

Abstract

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.