3w68

Crystal structure of mouse alpha-tocopherol transfer protein in complex with alpha-tocopherol and phosphatidylinositol-(4,5)-bisphosphate

spinqualitylabelsall models 3w68, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3w68 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: 4PT, PBU, PO4, VIV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TTPA_MOUSE Binds alpha-tocopherol and enhances its transfer between separate membranes (By similarity). Publication Abstract from PubMed alpha-Tocopherol (vitamin E) transfer protein (alpha-TTP) regulates the secretion of alpha-tocopherol from liver cells. Missense mutations of some arginine residues at the surface of alpha-TTP cause severe vitamin E deficiency in humans, but the role of these residues is unclear. Here, we found that wild-type alpha-TTP bound phosphatidylinositol phosphates (PIPs), whereas the arginine mutants did not. In addition, PIPs in the target membrane promoted the intermembrane transfer of alpha-tocopherol by alpha-TTP. The crystal structure of the alpha-TTP-PIPs complex revealed that the disease-related arginine residues interacted with phosphate groups of the PIPs and that the PIPs binding caused the lid of the alpha-tocopherol-binding pocket to open. Thus, PIPs have a role in promoting the release of a ligand from a lipid-transfer protein. Impaired alpha-TTP-PIPs Interaction Underlies Familial Vitamin E Deficiency.,Kono N, Ohto U, Hiramatsu T, Urabe M, Uchida Y, Satow Y, Arai H Science. 2013 Apr 18. PMID:23599266 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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