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.

doi:10.1126/science.2063194

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

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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ApoE2 has reduced binding affinity for the low density lipoprotein receptor.
“with apoE2 having reduced binding affinity for the low density lipoprotein (LDL) receptor [5]”
From Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice (2014) · cites this paper as [5]
The notion that apoE competes with Aβ for the same receptors may explain enhanced Aβ clearance in the setting of apoE2, which is defective in LDL receptor binding.
“This notion may explain enhanced Aβ clearance in the setting of apoE2, which is defective in LDL receptor binding [4,5].”
From Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice (2014) · cites this paper as [5]
The N-terminal domain of apoE is folded into a four-helix bundle of amphipathic alpha-helices spanning residues 24-164, stabilized by hydrophobic interactions and salt bridges.
“X-ray crystallography studies showed that the N-terminal domain is folded into a four-helix bundle of amphipathic α-helices spanning residues 24-164 that are stabilized by hydrophobic interactions and salt bridges [15], [16], [17].”
From Biophysical Analysis of Apolipoprotein E3 Variants Linked with Development of Type III Hyperlipoproteinemia (2011) · cites this paper as [15]
The seven-amino acid insertion in apoE Leiden occurs in a loop that connects helix 3 to helix 4 in the 4-helical bundle of the amino-terminal domain of apoE.
“The sevenamino acid insertion in apoE Leiden occurs in a loop that connectshelix 3 to helix 4 in the 4-helical bundle of the amino-terminal domain of apoE(25).”
From Preferential association of apolipoprotein E Leiden with very low density lipoproteins of human plasma. (1993) · cites this paper as [25]
X-ray crystallographic analysis of the lipid-free apoE amino-terminal domain (residues 1-191) showed a 4 helix bundle spanning residues 24-164 that segregates the hydrophobic core of the four helices from the solvent.
“X-ray crystallographic analysis of the lipid-free apoE amino-terminal domain (residues 1-191) showed a 4 helix bundle spanning residues 24 -164 that segregates the hydrophobic core of the four helices from the solvent (23).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [23]

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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
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Health Sciences › Medicine › Surgery › 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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