4p2j

Crystal structure of the mouse SNX19 PX domain with bound sulphate ion

spinqualitylabelsall models 4p2j, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p2j is a 2 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 2.4Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SNX19_MOUSE Plays a role in intracellular vesicle trafficking and exocytosis (PubMed:24843546). May play a role in maintaining insulin-containing dense core vesicles in pancreatic beta-cells and in preventing their degradation. May play a role in insulin secretion (PubMed:24843546). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:25148684). Publication Abstract from PubMed Sorting nexins (SNXs) or phox homology (PX) domain containing proteins are central regulators of cell trafficking and signaling. A sub-family of PX domain proteins possesses two unique PX-associated domains, as well as a regulator of GPCR signaling (RGS) domain that attenuates Galphas-coupled GPCR-signaling. Here we delineate the structural organization of these RGS-PX proteins, revealing a protein family with a modular architecture that is conserved in all eukaryotes. The one exception to this is mammalian SNX19, which lacks the typical RGS structure but preserves all other domains. The PX domain is a sensor of membrane phosphoinositide lipids and we find that specific sequence alterations in the PX domains of the mammalian RGS-PX proteins, SNX13, SNX14, SNX19 and SNX25, confer differential phosphoinositide binding preferences. While SNX13 and SNX19 PX domains bind the early endosomal lipid phosphatidylinositol 3-phosphate (PtdIns3P), SNX14 shows no membrane binding at all. Crystal structures of the SNX19 and SNX14 PX domains reveal key differences, with alterations in SNX14 leading to closure of the binding pocket to prevent phosphoinositide association. Our findings suggest a role for alternative membrane interactions in spatial control of RGS-PX proteins in cell signaling and trafficking. Structural basis for different phosphoinositide specificities of the PX domains of sorting nexins regulating G-protein signaling.,Mas C, Norwood SJ, Bugarcic A, Kinna G, Leneva N, Kovtun O, Ghai R, Ona Yanez LE, Davis JL, Teasdale RD, Collins BM J Biol Chem. 2014 Aug 22. pii: jbc.M114.595959. PMID:25148684 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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