Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E.
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Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA
Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E.
Science. 1991 Jun 28;252(5014):1817-22.
- PubMed ID
- 2063194 [ View in PubMed]
- 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.