Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E

Science. 1991 Jun 28;252(5014):1817-22. doi: 10.1126/science.2063194.


Human apolipoprotein E, a blood plasma protein, mediates the transport and uptake of cholesterol and lipid by way of its high affinity interaction with different cellular receptors, including the low-density lipoprotein (LDL) receptor. The three-dimensional structure of the LDL receptor-binding domain of apoE has been determined at 2.5 angstrom resolution by x-ray crystallography. The protein forms an unusually elongated (65 angstroms) four-helix bundle, with the helices apparently stabilized by a tightly packed hydrophobic core that includes leucine zipper-type interactions and by numerous salt bridges on the mostly charged surface. Basic amino acids important for LDL receptor binding are clustered into a surface patch on one long helix. This structure provides the basis for understanding the behavior of naturally occurring mutants that can lead to atherosclerosis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Apolipoproteins E / chemistry*
  • Apolipoproteins E / genetics
  • Apolipoproteins E / metabolism
  • Binding Sites
  • Computer Graphics
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, LDL / metabolism*
  • X-Ray Diffraction


  • Apolipoproteins E
  • Receptors, LDL