On the geometrical arrangement of the protein subunits of human serum low-density lipoprotein: evidence for a dodecahedral model.
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.
D000328:Adult; D006801:Humans; D008074:Lipoproteins / Q000097:blood*; D008297:Male; D008854:Microscopy, Electron; D008956:Models, Chemical; D008970:Molecular Weight; D013499:Surface Properties; D014461:Ultracentrifugation
D008074:Lipoproteins