β-sheet stabilization of the island domain underlies ligand-induced LRR-RP activation of plant immune signaling.

ABSTRACT: Leucine-rich repeat (LRR) receptor kinases (RKs) and receptor proteins (RPs) are important classes of plant pattern recognition receptors (PRRs) activating pattern-triggered immunity. While both classical and AI-based structural approaches have recently provided crucial insights into ligand-LRR-RK binding mechanisms, our understanding of ligand perception by LRR-RPs remains limited. Here, we employed an AI-based approach to reveal a ligand-binding mechanism shared by the Arabidopsis LRR-RPs RLP23 and RLP42 - the PRRs for the short peptide ligands nlp20 and pg13, derived from NECROSIS- AND ETHYLENE-INDUCING PEPTIDE 1-like proteins (NLPs) and fungal endopolygalacturonases (PGs), respectively. Additionally, we investigated the larger and more complex binding interface of RLP32 - the PRR for p

SUBMITTER: Snoeck S 

PROVIDER: S-EPMC12686451 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature