1LPE

THREE-DIMENSIONAL STRUCTURE OF THE LDL RECEPTOR-BINDING DOMAIN OF HUMAN APOLIPOPROTEIN E

Summary for 1LPE

• Entry DOI: 10.2210/pdb1lpe/pdb
• Descriptor: APOLIPOPROTEIN E3 (2 entities in total)
• Functional Keywords: lipoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02649
• Total number of polymer chains: 1
• Total formula weight: 16743.08

Authors

Wilson, C.,Agard, D.A. (deposition date: 1991-08-22, release date: 1992-10-15, Last modification date: 2024-02-14)

Primary citation

Wilson, C.,Wardell, M.R.,Weisgraber, K.H.,Mahley, R.W.,Agard, D.A.
Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E.
Science, 252:1817-1822, 1991

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.

PubMed: 2063194

Experimental method

X-RAY DIFFRACTION (2.25 Å)