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Article Dans Une Revue FEBS Letters Année : 2019

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

Résumé

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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Dates et versions

hal-02418813 , version 1 (25-11-2020)

Identifiants

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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, 2019, ⟨10.1002/1873-3468.13565⟩. ⟨hal-02418813⟩
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