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Related Experiment Videos

Cryo-electron microscopy reveals human low density lipoprotein substructure

R Van Antwerpen1, J C Gilkey

  • 1Department of Biochemistry, University of Arizona, Tucson 85721.

Journal of Lipid Research
|December 1, 1994
PubMed
Summary

Human low-density lipoprotein (LDL) particles are discoidal, not spherical. Cryo-electron microscopy revealed apolipoprotein B-100 forms ring structures in native LDL.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Low-density lipoprotein (LDL) is crucial for cholesterol transport.
  • Existing models depict LDL as spherical, but its native structure remains debated.

Purpose of the Study:

  • To determine the native structure of human LDL particles.
  • To investigate the distribution of apolipoprotein B-100 (apoB) within LDL.

Main Methods:

  • Cryo-electron microscopy was used to analyze human LDL.
  • Particles were examined in a vitrified frozen-hydrated state without chemical fixation or staining.

Main Results:

  • Human LDL particles exhibit a discoidal shape, contrary to spherical models.
  • Observed LDL disks measure 21.4 nm in diameter and 12.1 nm in height.

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  • Apolipoprotein B-100 appears to form two ring-like structures around the disk perimeter.

    • Conclusions:

    • The native structure of human LDL is discoidal.
    • The apoB distribution suggests a specific structural organization within the LDL particle.