Fig. 3: Structural changes from the outward-open conformation to the substrate-bound occluded conformation. | Nature Communications

Fig. 3: Structural changes from the outward-open conformation to the substrate-bound occluded conformation.

From: Mechanism of substrate recognition and release of human SGLT2

Fig. 3

a Superposition of the hSGLT2OO and hSGLT2SO. The mobile helices are shown as pink (hSGLT2OO) and blue(hSGLT2SO) cylinders respectively, and the less-mobile helices are shown as gray cylinders. The obvious movements of helices are shown as black arrows. b The rotation of a. The obvious movements of helices are shown as black arrows. c–h, Changes of polar interactions between the hSGLT2OO and hSGLT2SO, the color is the same as a. Helices are shown as cylinders. c, e, g, Extracellular polar interactions that maintain the occluded conformation of SGLT2. Dashed lines indicate hydrogen bonds and their distances. d, f, h The residues in the outward-facing conformation correspond to those in c, e, g. Dashed lines indicate the distances between residues that form hydrogen bonds in c, e, g, i, 1-NBD-glucose uptake (n ≥ 3 biologically independent experiments) and surface expression of hSGLT2 mutants in the presence of MAP17 (n = 2 biologically independent experiments). Data are normalized to WT hSGLT2-MAP17 (data are shown as means ± standard deviations). j 1-NBD-glucose uptake of hSGLT2-MAP17 mutants normalized by surface expression. The data are calculated using the mean of 1-NBD-glucose uptake divided by the mean of surface expression and normalized to WT hSGLT2-MAP17. Source data are provided as a Source Data file.

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