1n3k: Difference between revisions
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==Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)== | ==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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1n3k]] is a 1 chain structure with sequence from [http://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 [http:// | <table><tr><td colspan='2'>[[1n3k]] is a 1 chain structure with sequence from [http://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 [http://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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10029 CHO cell lines])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PEA15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10029 CHO cell lines])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n3k OCA], [http://pdbe.org/1n3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n3k RCSB], [http://www.ebi.ac.uk/pdbsum/1n3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n3k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cho cell lines]] | [[Category: Cho cell lines]] | ||
[[Category: Large Structures]] | |||
[[Category: Ginsberg, M H]] | [[Category: Ginsberg, M H]] | ||
[[Category: Hill, J M]] | [[Category: Hill, J M]] | ||
Revision as of 11:44, 2 December 2020
Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)
Structural highlights
Function[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.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPEA-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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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