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Trimeric structure of the mouse Kupffer cell C‐type lectin receptor Clec4f

Abstract : The C-type lectin receptor Clec4f has been identified as a specific surface marker for Kupffer cells, although its ortholog is absent in humans and its biological function remains elusive. Here, we report the crystal structure of a truncated mouse trimeric Clec4f. The orientation between the carbohydrate-recognition domain of Clec4f and its neck region differs from other C-type lectins, resulting in an observed distance of 45 Å between the glycan-binding sites within the Clec4f trimer. Interestingly, the trimeric coiled-coil interface within its heptad neck region contains multiple polyglutamine interactions instead of the predominantly hydrophobic leucine zipper found in other C-type lectin receptors. The Clec4f trimeric structure displays unique features regarding its assembly and ligand recognition, shedding light on the evolution and diversity of the C-type lectin family.
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Contributeur : Frank Thomas <>
Soumis le : jeudi 19 décembre 2019 - 10:34:27
Dernière modification le : mercredi 15 juillet 2020 - 13:02:04




Zhenlin Ouyang, Jan Felix, Jinhong Zhou, Yingmei Pei, Bohan Ma, et al.. Trimeric structure of the mouse Kupffer cell C‐type lectin receptor Clec4f. FEBS Letters, Wiley, 2019, ⟨10.1002/1873-3468.13565⟩. ⟨hal-02418813⟩



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