ArticleStructure (London, England : 1993)2013
Functional insights from the crystal structure of the N-terminal domain of the prototypical toll receptor.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- GABAPsychopharmacology · 2019Review
- TmToll-7 Plays a Crucial Role in Innate Immune Responses Against Gram-Negative Bacteria by Regulating 5 AMP Genes inFrontiers in immunology · 2019Article
- TLR Specific Immune Responses against Helminth Infections.Journal of parasitology research · 2017Review
- Structure of the OsSERK2 leucine-rich repeat extracellular domain.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Structure of the Toll-Spatzle complex, a molecular hub in Drosophila development and innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Conventional and non-conventional Drosophila Toll signaling.Developmental and comparative immunology · 2014Review
- Cytokine Spatzle binds to the Drosophila immunoreceptor Toll with a neurotrophin-like specificity and couples receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Liesegang-like patterns of Toll crystals grown in gel.Journal of applied crystallography · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Drosophila melanogaster Toll is the founding member of an important family of pathogen-recognition receptors in humans, the Toll-like receptor (TLR) family. In contrast, the prototypical receptor is a cytokine-like receptor for Spätzle (Spz) protein and plays a dual role in both development and immunity. Here, we present the crystal structure of the N-terminal domain of the receptor that encompasses the first 201 amino acids at 2.4 Å resolution. To our knowledge, the cysteine-rich cap adopts a novel fold unique to Toll-1 orthologs in insects and that is not critical for ligand binding. However, we observed that an antibody directed against the first ten LRRs blocks Spz signaling in a Drosophila cell-based assay. Supplemented by point mutagenesis and deletion analysis, our data suggests that the region up to LRR 14 is involved in Spz binding. Comparison with mammalian TLRs reconciles previous contradictory findings about the mechanism of Toll activation.
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