Fig. 4: The CQ binding site in 3d7-PfCRT and the interactions which support it. | Nature Communications

Fig. 4: The CQ binding site in 3d7-PfCRT and the interactions which support it.

From: Molecular basis of the functional conflict between chloroquine and peptide transport in the Malaria parasite chloroquine resistance transporter PfCRT

Fig. 4

A A side view of 3D7-PfCRT. B A top-down view of 3D7-PfCRT from the vacuolar side of the membrane. C A close-up of CQ in its 3D7-PfCRT binding site. CQ is shown in yellow, and residues whose average potential energy with CQ is in the top 5% of those <0 kJ mol−1, are colored in blue, and the those in the top 5% of an average potential energy >0 kJ mol−1 are colored in red. Transmembrane domain (TMD) alpha-helices are labeled. D The average potential energy between CQ at the 3D7-PfCRT binding site and a series of residues. The residues shown are those with the highest 5% of average potential energies, the lowest 5%, and residues that are mutated in Dd2-PfCRT as shown with an asterisks. Error bars represent the standard deviation of the potential energy. n = 8690 simulation frames in the binding site.

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