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. 2013 Apr 24;288(23):16598–16605. doi: 10.1074/jbc.M112.449306

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© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 2. — SNX11 interaction with PI3P and PI(3,5)P₂. A, superposition of critical residues in the PI-binding pocket of hSNX11-142C and p40^phox-PX. hSNX11-142C is shown as a white surface and cyan schematic. The side chains of residues that are critical for PI binding are shown for hSNX11-142C (green) and p40^phox-PX (blue). The sulfate in the PI-binding pocket of hSNX11-142C (show as a stick model: orange for sulfur and red for oxygen) coincides with the location of the 3-phosphate of PI3P from p40^phox-PX. B, the ability of His-tagged full-length (FL) SNX11, hSNX11-170C, and hSNX11-170C(R59A) to interact with various PIs was determined by lipid overlay assay. LPA, lysophosphatidic acid; LPC, lysophosphatidylcholine; PE, phosphatidylethanolamine; PC, phosphatidylcholine; S1P, sphingosine 1-phosphate; PI(3,4,5)P₃, PI 3,4,5-trisphosphate; PA, phosphatidic acid; PS, phosphatidylserine.