Apolipoprotein (apo) B-100 is a key protein compound of plasma lipid metabo
lism. This protein, as a sole component of LDL particles, to a great extent
controls the homeostasis of LDL cholesterol in the plasma. Therefore, this
protein and its structural variants play an important role in development
of hyperlipidemia and atherosclerosis. Intensive research into the structur
e and biological functions of apoB-100 has led to identification of its com
plete structure as well as the responsible binding sites. With the developm
ent of the methods of molecular biology, some structural variants of the ap
oB-100 protein that directly affect its binding properties have been descri
bed. These are mutations leading to amino acid substitution at positions 35
00 (R3500Q and R3500W) and 3531 (R3531C) that have been shown to decrease t
he binding affinity of apoB-100 in vitro. However, only the former mutation
s have been unequivocally demonstrated to cause hyperlipidemia in vivo. Thi
s minireview is aimed to discuss the impact of apoB-100 and its structural
variants on plasma lipid metabolism and development of hyperlipidemia.