1lpe
From Proteopedia
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THREE-DIMENSIONAL STRUCTURE OF THE LDL RECEPTOR-BINDING DOMAIN OF HUMAN APOLIPOPROTEIN E
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Alzheimer disease-2 OMIM:[107741], Hyperlipoproteinemia, type III OMIM:[107741], Macular degeneration, age-related OMIM:[107741], Myocardial infarction susceptibility OMIM:[107741], Sea-blue histiocyte disease OMIM:[107741]
About this Structure
1LPE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E., Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA, Science. 1991 Jun 28;252(5014):1817-22. PMID:2063194
Page seeded by OCA on Mon Nov 12 18:03:09 2007
