Fig. 1: Functional and structural analysis of XPR1.
From: Structure and function of human XPR1 in phosphate export
a Time-dependent phosphate export activity of cells transfected with wild-type HsXPR1 (WT) or empty vector (control). The data points are the mean ± s.e.m. (n = 6 independent experiments). b Phosphate export of HsXPR1 at 15 min from (a). P value from the two-tailed t-test is indicated on the bar chart. The data points are the mean ± s.e.m. (n = 6 independent experiments). c, d Cryo-EM density map (c) and cartoon representation (d) of XPR1 with each subunit depicted in an individual color. Lipid-like densities are colored gray. e The topology of XPR1. Dashed lines indicate the missing structural elements. f Structure of one XPR1 subunit. The scaffold domain (TM1-TM4) and core domain (TM5-TM10) are colored green and cyan, respectively. The potential phosphatidylcholine (purple) and its magnified EM density map (right panel) are shown.
