ArticleACS chemical biology2022
Identification of the Allosteric Binding Site for Thiazolopyrimidine on the C-Type Lectin Langerin.
Article in ACS chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026Review
- Article
- The Core-Shell Conformational Space of Compartmentalized Single-Chain Nanoparticles by Paramagnetic and Hyperpolarized NMR Spectroscopy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Calcium Competitive Inhibition of Langerin by Thiazolopyrimidinones.Journal of medicinal chemistry · 2025Article
- Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Glycomimetics for the inhibition and modulation of lectins.Chemical Society reviews · 2023Review
- Straight to the point: targeted mRNA-delivery to immune cells for improved vaccine design.Frontiers in immunology · 2023Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Langerin is a mammalian C-type lectin expressed on Langerhans cells in the skin. As an innate immune cell receptor, Langerin is involved in coordinating innate and adaptive immune responses against various incoming threats. We have previously reported a series of thiazolopyrimidines as murine Langerin ligands. Prompted by the observation that its human homologue exhibits different binding specificities for these small molecules, we report here our investigations to define their exact binding site. By using structural comparison and molecular dynamics simulations, we showed that the nonconserved short loops have a high degree of conformational flexibility between the human and murine homologues. Sequence analysis and mutational studies indicated that a pair of residues are essential for the recognition of the thiazolopyrimidines. Taking solvent paramagnetic relaxation enhancement NMR studies together with a series of peptides occupying the same site, we could define the cleft between the short and long loops as the allosteric binding site for these aromatic heterocycles.
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