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

FEBS Letters

article

Zhenlin Ouyang¹  Jan Felix³  Jinhong Zhou²  Yingmei Pei¹  Bohan Ma¹  Peter M. Hwang⁴  M. Joanne Lemieux⁴  Irina Gutsche⁶  Fang Zheng²  Yurong Wen¹ 

[1] The Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi'an Jiaotong University;Department of Biochemistry and Molecular Biology, The Key Laboratory of Environment and Genes Related to Disease of Ministry of Education, Health Science Center, Xi'an Jiaotong University;Institut de Biologie Structurale;Department of Biochemistry, Faculty of Medicine & Dentistry;Membrane Protein Disease Research Group, University of Alberta;Institut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS

关键词: Clec4f;    crystallography;    C-type lectin;    Kupffer cell receptor;    trimer;   

DOI  :  10.1002/1873-3468.13565

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown