Figure 1.

Structure of CD36. (Above) CD36 harbors two transmembrane domains, a large extracellular region containing ligand-binding sites, and one short cytoplasmic tail at each terminal (N and C). The extracellular domain of CD36 forms two hydrophobic cavities that bind to ligands such as fatty acids and oxidized LDL (ox-LDL). Moreover, the CLESH domain (CD36, LIMP-2, Emp sequence homologous domain) residues are negatively charged and interact with TSP-1 repeat domain 2 (TSR). CD36 undergoes multiple posttranslational modifications, including palmitoylation, acetylation, glycosylation, phosphorylation, ubiquitylation, and disulfide bonding (at three sites), and these modifications control CD36 maturation and localization in cells. Conversely, ligands bind to CD36 in different regions, and the binding leads to the activation of various downstream pathways. (Below) CD36 primary structure showing the hydrophobic domain and binding sites of general ligands. The numbers in different colors denote amino acid sites that undergo posttranslational modification: red, palmitoylation; green, glycosylation; blue, phosphorylation; dark blue, ubiquitylation; purple, acetylation.