 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](tb5105fig2mag.jpg)
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Figure 2
Interaction of LC3B and FYCO1 LIR. (a) Electrostatic surface potential of LC3B. The positively charged residues of LC3B are labelled. The bound FYCO1 LIR peptide is shown as a cartoon model with side chains of hydrophobic residues at positions 0, 3 and 8. Positive and negative electrostatic potential is shown in blue and red, respectively. The hydrophobic pockets, HP1 and HP2, are indicated. (b) Detailed view of the interactions between the hydrophobic pockets of LC3B and the hydrophobic residues of FYCO1 LIR. (c) Intermolecular main-chain interactions between LC3B and FYCO1 LIR. Hydrogen bonds are indicated by dashed lines. (d) Detailed view of the electrostatic interactions at the N-terminal (left) and C-terminal (right) extensions of the FYCO1 LIR motif. (e) Detailed view of the interaction of the C-terminal α-helix of FYCO1 LIR with LC3B. (f) Schematic summary of the interactions between LC3B and FYCO1 LIR. Hydrogen bonds and hydrophobic interactions are indicated by red and black dashed lines, respectively. The numbering scheme used in this paper is shown on the right. (g) GST pull-down assay using FYCO1 LIR fused to GST and LC3B. The input and eluted proteins were subjected to SDS–PAGE and stained with Coomassie Brilliant Blue. |
![[Figure 2]](tb5105fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
