Fig. 2: Overall structure of URAT1. | Cell Discovery

Fig. 2: Overall structure of URAT1.

From: Molecular mechanisms of urate transport by the native human URAT1 and its inhibition by anti-gout drugs

Fig. 2

a Structural comparisons of the inward-facing conformation of URAT1 with rOAT1 (PDB: 8SDY) and OCT1 (PDB: 8SC1). The NTD was used as a reference for structural alignments. b Electrostatic potential surfaces of URAT1 and OCT1 calculated in PyMOL (red to blue, −50 kT/e to +50 kT/e). The ECD and extracellular portions of the TMD bundle in URAT1 and OCT1 are shown. The circled region is positively charged in URAT1 and negatively charged in OCT1. c Cartoon representation of URAT1 highlighting the ECD and the ECD–TMD interface. Residues involved in ECD–TMD interactions are displayed, and cysteines participating in disulfide bond formation are shown as spheres. d 14C-urate uptake activities of mutants of pocket-forming residues relative to the wild-type URAT1. Data are shown as “mean values ± SEM.”; Four independent replicates were performed. Data were analyzed by two-sided, one-way ANOVA Tukey’s test. *P < 0.05, **P < 0.01, ***P < 0.001. Representative western blot images showing the expression of wild-type and mutant proteins. Na+/K+-ATPase is used as a loading control for cell surface proteins.

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