Fig. 2

Schematic representation of apoC1. A Structure of the transcribed region of the apoC1 gene. Exons are shown as boxes numbered with Roman numerals. Bold numbers are exon lengths, in nucleotides. Italicized numbers are intron lengths. The total length is indicated at the 3’-end of the gene. Beginning (ATG) and end (Stop) of translation are shown with black arrows. Untranslated and translated exonic sequences are shown in brown and green, respectively. B Primary structure of apoC1. Basic aminoacid residues are highlighted in dark blue for lysine and light blue for arginine. A lysine-rich cluster spans from residues 48 to 54. The vertical arrow represents the described possible site of truncation of apoC1 [35]. C Conformation of apoC1 with 2 α-helices according to [36] (permission validated by editor). The N-terminal helix spans from residues 7 to 29, the C-terminal helix from residue 38 to 52. The two helices are separated by an unstructured, hinge region. The conformation according to 2 or one α-helix might depend on the hydrophobicity of the environment. The blue frame delineates the region associated with the CETP-inhibitory effect. D Conformation of apoC1 with one α-helix with two possible dimeric associations according to [37] (permission validated by editor). Positively charged residues are shown in blue; negatively charged residues are shown in red. Hydrophobic clusters resulting from dimerization are visible as white/grey patches