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Structural heterogeneity of apolipoprotein B-100.

Altaira D Dearborn1, Alan T Remaley2, Joseph Marcotrigiano1

  • 1Structural Virology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.

The FEBS Journal
|February 17, 2026
PubMed
Summary

Researchers visualized the structure of apolipoprotein B-100 (apoB-100) on low-density lipoprotein (LDL) and its interaction with the low-density lipoprotein receptor (LDLR). This structural insight advances understanding of cardiovascular disease mechanisms.

Keywords:
LDLLDL receptorapolipoprotein B‐100cardiovascular diseasecholesterol

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Area of Science:

  • Structural Biology
  • Cardiovascular Science
  • Biochemistry

Background:

  • Cardiovascular disease (CVD) poses a significant global health burden, impacting morbidity and mortality.
  • Current drug strategies for CVD prevention often target the interaction between the low-density lipoprotein receptor (LDLR) and apolipoprotein B-100 (apoB-100) on low-density lipoprotein (LDL).
  • Understanding the structural basis of this interaction is crucial for developing effective therapies.

Purpose of the Study:

  • To determine the high-resolution structure of apoB-100 on LDL.
  • To elucidate the structural basis of apoB-100 interaction with LDLR.
  • To investigate structural heterogeneity and conformational flexibility of apoB-100.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the structure of apoB-100 on LDL.
  • Structural analysis was performed in both the absence and presence of LDLR.
  • Computational modeling and visualization techniques were utilized to interpret structural features.

Main Results:

  • The structure revealed that the C-terminal two-thirds of apoB-100 (>3000 residues) lack significant tertiary structure.
  • ApoB-100 forms amphipathic helices and β-sheets on the LDL surface, enveloping the lipid core.
  • The LDLR binding domain involves multiple sites on a circumferential β-belt and the N-terminus of apoB-100.
  • Structural heterogeneity and multiple conformations of apoB-100 were observed.

Conclusions:

  • The unique structural organization of apoB-100 facilitates its interaction with LDLR.
  • Observed conformational flexibility may enable apoB-100 to bind different lipoprotein sizes and interact with other molecules.
  • These findings provide critical structural insights into LDL metabolism and potential therapeutic targets for cardiovascular disease.