Key result
Cryo-EM and AlphaFold2 resolve human apoB100 structure, revealing a 61-nm belt wrapping LDL.
Why the study?
The size and complex lipid associations of apolipoprotein B100 have posed major challenges for structural studies of LDL.
Design
Integrative structural study using cryo-electron microscopy, AlphaFold2, and molecular-dynamics-based refinement
Authors
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Provides apoB100 structural template for LDL; leaves open translation to dyslipidemia therapies or atherosclerosis mechanisms.
Berndsen et al. (2024) studied this question. Cryo-electron microscopy and AlphaFold2 was evaluated. The structure of human apolipoprotein B100 was resolved using cryo-electron microscopy and AlphaFold2, revealing a globular N-terminal domain and a 61-nm-long beta-sheet belt wrapping the LDL particle.
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