1n3k: Difference between revisions

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 ==Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)==
-<StructureSection load='1n3k' size='340' side='right'caption='[[1n3k]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1n3k' size='340' side='right'caption='[[1n3k]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n3k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cho_cell_lines Cho cell lines]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N3K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n3k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N3K FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PEA15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10029 CHO cell lines])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1n3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n3k OCA], [https://pdbe.org/1n3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n3k RCSB], [https://www.ebi.ac.uk/pdbsum/1n3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n3k ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PEA15_CRIGR PEA15_CRIGR]] Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface (By similarity). Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm.<ref>PMID:9852038</ref> <ref>PMID:10982386</ref> <ref>PMID:14506247</ref>
+[https://www.uniprot.org/uniprot/PEA15_CRIGR PEA15_CRIGR] Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface (By similarity). Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm.<ref>PMID:9852038</ref> <ref>PMID:10982386</ref> <ref>PMID:14506247</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n3k ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-PEA-15 is a multifunctional protein that modulates signaling pathways which control cell proliferation and cell death. In particular, PEA-15 regulates the actions of the ERK MAP kinase cascade by binding to ERK and altering its subcellular localization. The three-dimensional structure of PEA-15 has been determined using NMR spectroscopy and its interaction with ERK defined by characterization of mutants that modulate ERK function. PEA-15 is composed of an N-terminal death effector domain (DED) and a C-terminal tail of irregular structure. NMR 'footprinting' and mutagenesis identified elements of both the DED and tail that are required for ERK binding. Comparison of the DED-binding surface for ERK2 with the death domain (DD)-binding surface of Drosophila Tube revealed an unexpected similarity between the interaction modes of the DD and DED motifs in these proteins. Despite a lack of functional or sequence similarity between PEA-15 and Tube, these proteins utilize a common surface of the structurally similar DD and DED to recognize functionally diverse targets.
-Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain.,Hill JM, Vaidyanathan H, Ramos JW, Ginsberg MH, Werner MH EMBO J. 2002 Dec 2;21(23):6494-504. PMID:12456656<ref>PMID:12456656</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1n3k" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Cho cell lines]]
+[[Category: Cricetulus griseus]]
 [[Category: Large Structures]]
-[[Category: Ginsberg, M H]]
+[[Category: Ginsberg MH]]
-[[Category: Hill, J M]]
+[[Category: Hill JM]]
-[[Category: Ramos, J W]]
+[[Category: Ramos JW]]
-[[Category: Vaidyanathan, H]]
+[[Category: Vaidyanathan H]]
-[[Category: Werner, M H]]
+[[Category: Werner MH]]
-[[Category: Apoptosis]]
-[[Category: Death effector domain]]
-[[Category: Six helix bundle]]