6JJJ

Trimeric structure of Kupffer cell C-type lectin receptor Clec4f

Summary for 6JJJ

• Entry DOI: 10.2210/pdb6jjj/pdb
• Descriptor: C-type lectin domain family 4 member F, CALCIUM ION (3 entities in total)
• Functional Keywords: c-type lectin receptor, clec4f, kupffer cell receptor, sugar binding protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 6
• Total formula weight: 110791.98

Authors

Wen, Y.,Ouyang, Z.,Felix, J. (deposition date: 2019-02-26, release date: 2019-08-14, Last modification date: 2024-11-06)

Primary citation

Ouyang, Z.,Felix, J.,Zhou, J.,Pei, Y.,Ma, B.,Hwang, P.M.,Lemieux, M.J.,Gutsche, I.,Zheng, F.,Wen, Y.
Trimeric structure of the mouse Kupffer cell C-type lectin receptor Clec4f.
Febs Lett., 594:189-198, 2020

PubMed 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.

PubMed: 31369681
DOI: 10.1002/1873-3468.13565

Experimental method

X-RAY DIFFRACTION (2.792 Å)