Figure 2 | Scientific Reports

Figure 2

From: Solution structure of the autophagy-related protein LC3C reveals a polyproline II motif on a mobile tether with phosphorylation site

Figure 2

Solution structure of LC3C shown as a superposition of the backbone traces of the 10 accepted structures with a schematic representation of the secondary structure elements as identified with DSSP99. The tertiary structure of LC3C consists of three α-helices (α2: Leu19 to Lys32, α3: Met66 to Arg76, α4: Met101 to Tyr108; red) and a central β-sheet of four β-strands (β1: Lys36 to Arg43, β2: Lys57 to Pro61, β3: Tyr86 to Val89, β4: Val115 to Ala120; blue). In the ubiquitin-like core of the protein the 10 accepted structures are in excellent agreement, whereas the amino (N) and carboxy (C) termini as well as some of the loops are highly flexible in solution. The location of the two hydrophobic pockets is indicated by hp1 and hp2. The overlay was performed using PyMOL (The PyMOL Molecular Graphics System, Version 1.7.2.1, Schrödinger, LLC).

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