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Trimeric structure of the mouse Kupffer cell C-type lectin receptor Clec4f
Zhenlin Ouyang1,2, Jan Felix3, Jinhong Zhou2
1The Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi'an Jiaotong University, China.
FEBS Letters
|August 2, 2019
Summary
The C-type lectin receptor Clec4f, a Kupffer cell marker, has a unique structure in mice. Its distinct trimeric assembly and ligand binding sites offer insights into C-type lectin evolution.
Area of Science:
- Immunology
- Structural Biology
- Biochemistry
Background:
- Clec4f is a C-type lectin receptor and a specific surface marker for Kupffer cells.
- Its human ortholog is absent, and its biological function is not well understood.
- Understanding Clec4f structure is crucial for deciphering its role in Kupffer cell biology.
Purpose of the Study:
- To determine the crystal structure of a truncated mouse Clec4f trimer.
- To elucidate the structural basis for Clec4f assembly and ligand recognition.
- To provide insights into the evolution and diversity of C-type lectin receptors.
Main Methods:
- X-ray crystallography was used to obtain the crystal structure of truncated mouse Clec4f.
- Structural analysis focused on the orientation of the carbohydrate-recognition domain and neck region.
- Comparison of the trimeric coiled-coil interface with other C-type lectin receptors.
Main Results:
- The crystal structure of a truncated mouse Clec4f trimer was determined.
- Clec4f exhibits a unique orientation between its carbohydrate-recognition domain and neck region, with a 45 Å distance between glycan-binding sites.
- The trimeric interface features polyglutamine interactions, differing from the typical leucine zipper in other C-type lectin receptors.
Conclusions:
- The unique structural features of Clec4f suggest novel mechanisms for assembly and ligand binding.
- These findings contribute to understanding the diversity within the C-type lectin family.
- Further research on Clec4f function is warranted given its distinct structural characteristics.
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