4xpn: Difference between revisions

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 ==Crystal Structure of Protein Phosphate 1 complexed with PP1 binding domain of GADD34==
-<StructureSection load='4xpn' size='340' side='right' caption='[[4xpn]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
+<StructureSection load='4xpn' size='340' side='right'caption='[[4xpn]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4xpn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XPN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4xpn]] 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=4XPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XPN 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>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.285&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></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>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4xpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpn OCA], [http://pdbe.org/4xpn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xpn RCSB], [http://www.ebi.ac.uk/pdbsum/4xpn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xpn ProSAT]</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=4xpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpn OCA], [https://pdbe.org/4xpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xpn RCSB], [https://www.ebi.ac.uk/pdbsum/4xpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xpn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PP1A_HUMAN PP1A_HUMAN]] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.<ref>PMID:17283141</ref>  [[http://www.uniprot.org/uniprot/PR15A_HUMAN PR15A_HUMAN]] Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'.<ref>PMID:11564868</ref> <ref>PMID:12556489</ref> <ref>PMID:14635196</ref> <ref>PMID:14718519</ref> <ref>PMID:8139541</ref>
+[https://www.uniprot.org/uniprot/PR15A_HUMAN PR15A_HUMAN] Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'.<ref>PMID:11564868</ref> <ref>PMID:12556489</ref> <ref>PMID:14635196</ref> <ref>PMID:14718519</ref> <ref>PMID:8139541</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 </div>
 <div class="pdbe-citations 4xpn" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Homo sapiens]]
-[[Category: Choy, M S]]
+[[Category: Large Structures]]
-[[Category: Page, R]]
+[[Category: Choy MS]]
-[[Category: Peti, W]]
+[[Category: Page R]]
-[[Category: Eif2alpha phosphatase]]
+[[Category: Peti W]]
-[[Category: Hydrolase]]
-[[Category: Pp1 regulator]]