The Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi'an Jiaotong University, China.
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, China.
FEBS Lett. 2020 Jan;594(1):189-198. doi: 10.1002/1873-3468.13565. Epub 2019 Aug 9.
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.
C 型凝集素受体 Clec4f 已被鉴定为枯否细胞的特异性表面标志物，尽管其同源物在人类中不存在，其生物学功能仍不清楚。在这里，我们报告了一种截断的小鼠三聚体 Clec4f 的晶体结构。Clec4f 的碳水化合物识别域与其颈部区域之间的取向不同于其他 C 型凝集素，导致在 Clec4f 三聚体中观察到糖结合位点之间的距离为 45 Å。有趣的是，其七肽颈区的三聚体卷曲螺旋界面包含多个多聚谷氨酰胺相互作用，而不是在其他 C 型凝集素受体中发现的主要疏水性亮氨酸拉链。Clec4f 三聚体结构在其组装和配体识别方面表现出独特的特征，为 C 型凝集素家族的进化和多样性提供了线索。
