Fig. 2: The urate-binding site of hURAT1.
From: Mechanisms of urate transport and uricosuric drugs inhibition in human URAT1
a The chemical structure of urate at a physiological pH. b A cut-open view of the urate-binding site of hURAT1. The surface of hURAT1 is colored by the electrostatic potential calculated using Pymol. Urate is shown as cyan spheres. c Electron densities of urate and nearby residues. The map is shown as grey surface, contoured at 5 σ. Urate is shown as cyan sticks. The nearby residues are colored the same as in Fig. 1f. d, e Interactions between urate and hURAT1. Urate and its interacting residues are shown as sticks. Putative polar interactions are depicted as black dashed lines. f Urate uptake activities of various hURAT1 mutants. Data are normalized to hURAT1WT, shown as means ± s.d.; n = 3 technical replicates. The experiment was performed independently twice with similar results. Statistical significance compared with hURAT1WT was determined using ordinary one-way ANOVA with Dunnett’s multiple comparisons test. ***P < 0.001, ****P < 0.0001. P value of normalized uptake efficiency between hURAT1WT and the mutant F360A is 0.0003. g Surface expression of various hURAT1 mutants. Data are normalized to hURAT1WT, shown as means ± s.d.; n = 3 technical replicates. The experiment was performed independently twice with similar results. Statistical significance compared with hURAT1WT was determined using ordinary one-way ANOVA with Dunnett’s multiple comparisons test. ****P < 0.0001.
