1991/06/28 by Charles B. Wilson, Mark R. Wardell, Karl H. Weisgraber +2 · 2 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Computer Science · Medicine · #Apolipoprotein B #Apolipoprotein E #Biochemistry #Biology #Biophysics #Chemistry #Cholesterol #Computational Drug Discovery Methods #Crystallography #Helix (gastropod) #Helix bundle #Internal medicine #LDL receptor #Leucine zipper #Lipoprotein #Lipoproteins and Cardiovascular Health #Peptide sequence #Plasma protein binding #Protein Structure and Dynamics #Protein structure #Receptor
paper · doi:10.1126/science.2063194
openalex publication_date 1991/06/28 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/23
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.