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Publication Abstract from PubMed

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 A 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.

Trimeric structure of the mouse Kupffer cell C-type lectin receptor Clec4f.,Ouyang Z, Felix J, Zhou J, Pei Y, Ma B, Hwang PM, Lemieux MJ, Gutsche I, Zheng F, Wen Y FEBS Lett. 2019 Aug 1. doi: 10.1002/1873-3468.13565. PMID:31369681^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.