Structural characteristics of alpha-fetoprotein, including N-glycosylation, metal ion and fatty acid binding sites.
Commun Biol
; 7(1): 505, 2024 Apr 27.
Article
in En
| MEDLINE
| ID: mdl-38678117
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Alpha-Fetoproteins
/
Models, Molecular
/
Fatty Acids
Limits:
Humans
Language:
En
Journal:
Commun Biol
Year:
2024
Document type:
Article
Country of publication:
United kingdom