Cited by 678Protein Structure and DynamicsEnzyme Structure and FunctionLipoproteins and Cardiovascular Health

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Three-Dimensional Structure of the LDL Receptor-Binding Domain of Human Apolipoprotein E

Wilson, Charles, Wardell, Mark R., Weisgraber, Karl H., Mahley, Robert W., Agard, David A.·1991·Science

DOI 10.1126/science.2063194

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Abstract

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.

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Authors: Wilson, C., Wardell, M. R., Weisgraber, K. H., Mahley, R. W., & Agard, D. A.
Affiliations: Howard Hughes Medical Institute (US)
University of California, San Francisco (US)
ORCID: Mahley, Robert W.
Agard, David A.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1991-06-28
Volume: 252
Issue: 5014
Pages: 1817-1822
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.2063194
OpenAlex: W1994543234
Cited by: 678
References: 41
Citations by year: 2026: 11 · 2025: 14 · 2024: 11 · 2023: 18 · 2022: 10 · 2021: 11 · 2020: 9 · 2019: 13 · 2018: 12 · 2017: 15 · 2016: 15 · 2015: 9 · 2014: 24 · 2013: 13 · 2012: 19
FWCI: 9.38
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (HL-41633, P01HL041633)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
Keywords: apolipoprotein E, protein structure, four-helix bundle, hydrophobic core, leucine zipper, salt bridges, basic amino acid clusters, atherosclerosis, cholesterol transport, ligand-receptor interactions
MeSH terms: Amino Acid Sequence, Apolipoproteins E, Binding Sites, Computer Graphics, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Receptors, LDL, X-Ray Diffraction

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Three-Dimensional Structure of the LDL Receptor-Binding Domain of Human Apolipoprotein E

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