ArticleActa crystallographica. Section D, Structural biology2019
Crystal structure of the leucine-rich repeat ectodomain of the plant immune receptor kinase SOBIR1.
Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Structure of the Arabidopsis receptor kinase SRF6 ectodomain determined from crystals obtained using the LRR crystallization screen.Acta crystallographica. Section D, Structural biology · 2026Article
- Plant structural biology: Emerging technologies and future biological insights.The Plant journal : for cell and molecular biology · 2026Review
- Plant cell surface receptors.The Plant journal : for cell and molecular biology · 2026Review
- Pattern-Triggered Immunity and Effector-Triggered Immunity: crosstalk and cooperation of PRR and NLR-mediated plant defense pathways during host-pathogen interactions.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Review
- Evolutionary gain and loss of a plant pattern-recognition receptor for HAMP recognition.eLife · 2022Article
- Structural analysis of receptor-like kinase SOBIR1 reveals mechanisms that regulate its phosphorylation-dependent activation.Plant communications · 2022Article
- A molecular roadmap to the plant immune system.The Journal of biological chemistry · 2020Review
- Direct evidence for a new mode of plant defense against insects via a novel polygalacturonase-inhibiting protein expression strategy.The Journal of biological chemistry · 2020Article
- Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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2 authors at 1 institution in 1 country.
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Abstract
Plant-unique membrane receptor kinases with leucine-rich repeat (LRR) extracellular domains are key regulators of development and immune responses. Here, the 1.55 Å resolution crystal structure of the immune receptor kinase SOBIR1 from Arabidopsis is presented. The ectodomain structure reveals the presence of five LRRs sandwiched between noncanonical capping domains. The disulfide-bond-stabilized N-terminal cap harbours an unusual β-hairpin structure. The C-terminal cap features a highly positively charged linear motif which was found to be largely disordered in this structure. Size-exclusion chromatography and right-angle light-scattering experiments suggest that SOBIR1 is a monomer in solution. The protruding β-hairpin, a set of highly conserved basic residues at the inner surface of the SOBIR LRR domain and the presence of a genetic missense allele in LRR2 together suggest that the SOBIR1 ectodomain may mediate protein-protein interaction in plant immune signalling.
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