4pqp: Difference between revisions

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 ==Crystal structure of human SNX14 PX domain in space group P43212==
-<StructureSection load='4pqp' size='340' side='right' caption='[[4pqp]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='4pqp' size='340' side='right'caption='[[4pqp]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4pqp]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PQP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4pqp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PQP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pqo|4pqo]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqp RCSB], [http://www.ebi.ac.uk/pdbsum/4pqp PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqp OCA], [https://pdbe.org/4pqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pqp RCSB], [https://www.ebi.ac.uk/pdbsum/4pqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pqp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SNX14_HUMAN SNX14_HUMAN]] May be involved in several stages of intracellular trafficking (By similarity).
+[https://www.uniprot.org/uniprot/SNX14_HUMAN SNX14_HUMAN] May be involved in several stages of intracellular trafficking (By similarity).
-<div style="background-color:#fffaf0;">
-== 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<ref>PMID:25148684</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bugarcic, A]]
+[[Category: Homo sapiens]]
-[[Category: Collins, B]]
+[[Category: Large Structures]]
-[[Category: Kinna, G]]
+[[Category: Bugarcic A]]
-[[Category: Kovtun, O]]
+[[Category: Collins B]]
-[[Category: Leneva, N]]
+[[Category: Kinna G]]
-[[Category: Mas, C]]
+[[Category: Kovtun O]]
-[[Category: Norwood, S]]
+[[Category: Leneva N]]
-[[Category: Teasdale, R]]
+[[Category: Mas C]]
-[[Category: Phosphoinositide binding]]
+[[Category: Norwood S]]
-[[Category: Phox homology domain]]
+[[Category: Teasdale R]]
-[[Category: Protein transport]]
-[[Category: Sorting nexin]]