A model of human APOA2 on HDL
Yi He, Hyun Song, Youngki You, John T Melchior, Martin K Jones, Stephen G Aller, W Sean Davidson, Jay W Heinecke, Jere P Segrest · 2026
Read A model of human APOA2 on HDL by Yi He, Hyun Song, Youngki You, John T Melchior, Martin K Jones, Stephen G Aller, W Sean Davidson, Jay W Heinecke, Jere P Segrest (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13505420.txt.
Description
Yi He and colleagues built a structural model of apolipoprotein A-II, the second most common protein carried on HDL, the particles that move cholesterol out of tissues. The protein grips lipids more tightly than its better-known partner APOA1, yet its shape on the particle was unsettled. The team combined computer modelling with targeted mutations to test how the chain folds.
Their model wraps the protein's paired chains as a double hairpin belt around disc-shaped HDL. Most charged building blocks sit in the hairpin loop, and internal bridges plus ring stacking hold the fold steady. Two strong lipid-binding stretches appear in each half of the pair, and the hairpin seems built to meet partner proteins. Chemical crosslinking found sixteen links between parts of the chain, and fifteen of them fit the belt model. The result gives lipid researchers a picture for explaining how APOA2 shapes HDL behaviour.
Catalog record
| CREATOR | Yi He, Hyun Song, Youngki You, John T Melchior, Martin K Jones, Stephen G Aller, W Sean Davidson, Jay W Heinecke, Jere P Segrest |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 46 KB |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |