Journal
FEBS LETTERS
Volume 594, Issue 1, Pages 189-198Publisher
WILEY
DOI: 10.1002/1873-3468.13565
Keywords
Clec4f; crystallography; C-type lectin; Kupffer cell receptor; trimer
Funding
- National Natural Science Foundation of China [31870132, 81741088, 31500051]
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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 angstrom 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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