The study presents the first structure of Apolipoprotein B100 (apoB100) resolved to sub-nanometer resolution, revealing critical insights into LDL and its role in atherosclerosis.
The structural analysis indicates that the large globular N-terminal domain and the continuous amphipathic β-sheet provide essential stability and cohesion to the LDL particle.
Using an integrative approach combining cryo-electron microscopy, AlphaFold2, and molecular dynamics refinement, the research delineates apoB100's complex role in maintaining LDL shape.
By comparing the new structure to over 200 intramolecular crosslinks, the findings bolster our understanding of LDL’s structural dynamics and pathophysiological relevance.
#apolipoprotein-b100 #ldl-cholesterol #atherosclerosis #cryo-electron-microscopy #structural-biology
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