The assembly of apoB-containing lipoproteins: A structural biology point of view

Abstract

Atherosclerosis is a widespread disease caused by the deposition of lipids on arterial walls. Such lipid plaques in coronary arteries can be fatal. Although many factors related to diet, life-style, etc. contribute to the worsening of the ailment, the primary cause, the lipids in the circulatory system, come from a series of low-density lipoproteins. These lipoproteins are necessary for the transport of lipids to and from different organs. It would be valuable to medicine and the field of drug design if a more detailed understanding of the organization of lipid and protein in these molecules were available. Unfortunately because of heterogeneity in their size and lipid composition, all classes of the low-density serum lipoproteins appear to be not amenable to the most widely used method for obtaining detailed atomic data—X-ray crystallography. However there appears to be a recently identified homolog that is relatively homogeneous, and crystal structures have been obtained. Used as a molecular model, the homolog serves as a source of conformational information that might help to unravel the processes involved in the lipid loading of the low-density lipoproteins. The review attempts to give a brief summary of the structural biology of the serum low-density lipoproteins relative to the molecular model of lipovitellin.