Fig. 5: The Dd2-PfCRT CQ binding site and the interactions which support it. | Nature Communications

Fig. 5: The Dd2-PfCRT CQ binding site 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. 5

A A side view of Dd2-PfCRT and the two minimum free energy paths as calculated by MULE from bulk solution to the CQ binding site. B A top down view from the vacuolar side of the membrane, of the CQ binding site in Dd2-PfCRT. C A close-up of CQ in its Dd2-PfCRT binding site. The residues with the lowest and highest 5% average potential energies are colored blue and red, respectively. The two minimum free energy paths that CQ can take to the binding site are also displayed and each CQ position colored on a blue to red scale, with blue being low free energy. Transmembrane domain (TMD) alpha-helices are labeled. D The average potential energy between CQ at the Dd2-PfCRT binding site and a series of residues. The residues shown are those with the lowest and highest 5% average potential energies, and also those that are mutated in Dd2-PfCRT and are marked with an asterisk. Error bars represent the standard deviation of the potential energy. n = 1190 simulation frames in the binding site.

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