{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Snoeck S"],"funding":["Swiss National Science Foundation","Universität Zürich (University of Zurich)","Deutsche Forschungsgemeinschaft (German Research Foundation)","European Molecular Biology Organization (EMBO)"],"pagination":["10958"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12686451"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_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"],"journal":["Nature communications"],"pubmed_title":["β-sheet stabilization of the island domain underlies ligand-induced LRR-RP activation of plant immune signaling."],"pmcid":["PMC12686451"],"funding_grant_id":["n/a","ALTF 580-2022","K-74503-08-01","TMPFP3_224980","Nu70/19-1","CRC1101-D10"],"pubmed_authors":["Nurnberger T","Kim G","Snoeck S","Zhang L","Zipfel C","Fernandez-Fernandez AD","Studer V"],"additional_accession":[]},"is_claimable":false,"name":"β-sheet stabilization of the island domain underlies ligand-induced LRR-RP activation of plant immune signaling.","description":"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","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-05T23:55:32.533Z","creation":"2026-05-23T03:13:48.482Z"},"accession":"S-EPMC12686451","cross_references":{"pubmed":["41361182"],"doi":["10.1038/s41467-025-66119-7"]}}