Conformational plasticity and dynamic interactions of the N-terminal domain of the chemokine receptor CXCR1
Fig 1
Representative snapshots of CXCR1 embedded in a lipid bilayer and membrane interaction of its N-terminal region.
A visual representation of (A) the starting conformation with an extended N-terminal region, (B) the membrane-embedded N-terminal conformer and (C) the receptor-contacted N-terminal conformer. The receptor is depicted in magenta, the N-terminal region in orange, and the lipid headgroups and tails in yellow and gray, respectively. Water and ions are not displayed for clarity. The residue W10 of the N-terminal region, which interacts with the lipid bilayer is shown as cyan colored beads. (D) The minimum distance between the lipid bilayer and the distal part of the N-terminal region (residues 1–10) is plotted for 20 simulations of apo-CXCR1 as a function of time. The color bar denotes minimum distance in nm. A distance of ~0.4 nm (dark blue patches) indicates the binding of the N-terminal region to the lipid bilayer. (E) The radius of gyration of the N-terminal region is plotted for apo-CXCR1 as a function of time. The color bar denotes radius of gyration in nm. See Methods for more details.