Figure 1 CD36 structure and post-translational modifications

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Figure 1 CD36 structure and post-translational modifications Figure 1 | CD36 has two transmembrane domains and two small cytoplasmic tails that contain four palmitoylation sites. The C-terminus contains two ubiquitylation sites and the N-terminal transmembrane domain contains two motifs (G12xxxG16xxxA20 and A20xxG23) that are responsible for dimerization. The large extracellular loop contains ten N-linked glycosylation sites and two phosphorylation sites. CD36 also contains a ~30-residue-long CD36, LIMP-2, Emp sequence homology (CLESH) domain. A variety of ligands bind to CD36 via the hydrophobic binding pocket (entrance 1). Crystal structure studies also suggest that CD36 might have a second entrance (entrance 2) for fatty acid transport. Yang, X. et al. (2017) CD36 in chronic kidney disease: novel insights and therapeutic opportunities Nat. Rev. Nephrol. doi:10.1038/nrneph.2017.126