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. 1969 Sep;64(1):304–310. doi: 10.1073/pnas.64.1.304

ON THE GEOMETRICAL ARRANGEMENT OF THE PROTEIN SUBUNITS OF HUMAN SERUM LOW-DENSITY LIPOPROTEIN: EVIDENCE FOR A DODECAHEDRAL MODEL*

H Pollard 1,2,3,4,†, A M Scanu 1,2,3,4,‡, E W Taylor 1,2,3,4,§
PMCID: PMC286162  PMID: 5263015

Abstract

Ultracentrifugal and electron microscopic studies of human serum low-density lipoprotein (LDL) and several of its derivatives led to the formulation of a model in which the 20 protein subunits, probably globular, are arranged in a dodecahedral pattern with icosahedral symmetry. In such a model the LDL surface is occupied by both protein and lipids, predominantly phospholipids, as supported by the results of the hydrolysis of LDL by phospholipase A and C. Neutral lipids (cholesterol esters and glycerides) would be in the interior of the molecule.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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