8X1N

Cryo-EM structure of human alpha-fetoprotein

Summary for 8X1N

• Entry DOI: 10.2210/pdb8x1n/pdb
• EMDB information: 37997
• Descriptor: Alpha-fetoprotein, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (4 entities in total)
• Functional Keywords: n-glycosylation, fatty acids, metal ion, transport protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 70435.05

Authors

Liu, Z.M.,Li, M.S.,Wu, C.,Liu, K. (deposition date: 2023-11-08, release date: 2024-05-15, Last modification date: 2024-10-16)

Primary citation

Liu, K.,Wu, C.,Zhu, M.,Xu, J.,Lin, B.,Lin, H.,Liu, Z.,Li, M.
Structural characteristics of alpha-fetoprotein, including N-glycosylation, metal ion and fatty acid binding sites.
Commun Biol, 7:505-505, 2024

PubMed 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.

PubMed: 38678117
DOI: 10.1038/s42003-024-06219-0

Experimental method

ELECTRON MICROSCOPY (3.31 Å)