2. Academic Validation
  3. Structural characteristics of alpha-fetoprotein, including N-glycosylation, metal ion and fatty acid binding sites

Structural characteristics of alpha-fetoprotein, including N-glycosylation, metal ion and fatty acid binding sites

  • Commun Biol. 2024 Apr 27;7(1):505. doi: 10.1038/s42003-024-06219-0.
Kun Liu # 1,  Cang Wu # 2,  Mingyue Zhu # 1,  Junnv Xu # 1 3,  Bo Lin 1,  Haifeng Lin 3,  Zhongmin Liu 4,  Mengsen Li 5 6 7
Affiliations

Affiliations

  • 1 Hainan Provincial Key Laboratory of Carcinogenesis and Intervention, Hainan Medical College, Haikou, 571199, Hainan, PR China.
  • 2 Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, Guangdong, PR China.
  • 3 Department of Medical Oncology, Second Affiliated Hospital, Hainan Medical College, Haikou, 570023, Hainan, PR China.
  • 4 Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, Guangdong, PR China. liuzm@sustech.edu.cn.
  • 5 Hainan Provincial Key Laboratory of Carcinogenesis and Intervention, Hainan Medical College, Haikou, 571199, Hainan, PR China. mengsenli@163.com.
  • 6 Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, Guangdong, PR China. mengsenli@163.com.
  • 7 Institution of Tumor, Hainan Medical College, Haikou, 570102, Hainan, PR China. mengsenli@163.com.
  • # Contributed equally.
PMID: 38678117 DOI: 10.1038/s42003-024-06219-0
Abstract

Alpha-fetoprotein (AFP), a serum glycoprotein, is expressed during embryonic development and the pathogenesis of liver Cancer. It serves as a clinical tumor marker, function as a carcinogen, immune suppressor, and transport vehicle; but the detailed AFP structural information has not yet been reported. In this study, we used single-particle cryo-electron microscopy(cryo-EM) to analyze the structure of the recombinant AFP obtained a 3.31 Å cryo-EM structure and built an atomic model of AFP. We observed and identified certain structural features of AFP, including N-glycosylation at Asn251, four natural fatty acids bound to distinct domains, and the coordination of metal ions by residues His22, His264, His268, and Asp280. Furthermore, we compared the structural similarities and differences between AFP and human serum albumin. The elucidation of AFP's structural characteristics not only contributes to a deeper understanding of its functional mechanisms, but also provides a structural basis for developing AFP-based drug vehicles.

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