Fig. 5: Free energy calculations for different hKir channels. | Communications Chemistry

Fig. 5: Free energy calculations for different hKir channels.

From: Evaluating inositol phospholipid interactions with inward rectifier potassium channels and characterising their role in disease

Fig. 5: Free energy calculations for different hKir channels.

a Models of a hKir1.1, b hKir2.2, and c hKir3.2 channels in the PIP2-bound conformations after 1 μs of CG simulation and converted back to an atomistic description. Insets: carbons of key PIP2-binding residues are highlighted in yellow, with PIP2 otherwise shown in CPK colours. d Sequence alignment between hKir1.1, hKir2.2, hKir3.2, and hKir6.2 channels on the region where the contacts are conserved between more than two channels. Highlighted in yellow are residues that contact PIP2 for >70% of the 1 μs simulations (n = 5). Long cylinder represents an α-helix in the secondary structure and the line represents either disordered region or a kink within the α-helix. Acidic residues (Asp, Glu) are shown in red, basic residues (Lys, Arg) are shown in blue, and polar residues (His, Ser, Thr, Cys, Gln, Asn) are shown in green. Other residues are shown in black.

Back to article page