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| | ==Structure of 14-3-3 gamma R57E mutant bound to GlcNAcylated peptide== | | ==Structure of 14-3-3 gamma R57E mutant bound to GlcNAcylated peptide== |
| - | <StructureSection load='6bzd' size='340' side='right' caption='[[6bzd]], [[Resolution|resolution]] 2.67Å' scene=''> | + | <StructureSection load='6bzd' size='340' side='right'caption='[[6bzd]], [[Resolution|resolution]] 2.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6bzd]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BZD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bzd]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BZD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.67Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5usm|5usm]], [[5usk|5usk]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YWHAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6bzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bzd OCA], [https://pdbe.org/6bzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bzd RCSB], [https://www.ebi.ac.uk/pdbsum/6bzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bzd ProSAT]</span></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=6bzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bzd OCA], [http://pdbe.org/6bzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bzd RCSB], [http://www.ebi.ac.uk/pdbsum/6bzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bzd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/1433G_HUMAN 1433G_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:16511572</ref> | + | [https://www.uniprot.org/uniprot/1433G_HUMAN 1433G_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:16511572</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6bzd" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6bzd" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Schumacher, M A]] | + | [[Category: Large Structures]] |
| - | [[Category: Reader protein]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Signaling protein]] | + | [[Category: Schumacher MA]] |
| Structural highlights
Function
1433G_HUMAN Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.[1]
Publication Abstract from PubMed
O-GlcNAc is an intracellular posttranslational modification that governs myriad cell biological processes and is dysregulated in human diseases. Despite this broad pathophysiological significance, the biochemical effects of most O-GlcNAcylation events remain uncharacterized. One prevalent hypothesis is that O-GlcNAc moieties may be recognized by "reader" proteins to effect downstream signaling. However, no general O-GlcNAc readers have been identified, leaving a considerable gap in the field. To elucidate O-GlcNAc signaling mechanisms, we devised a biochemical screen for candidate O-GlcNAc reader proteins. We identified several human proteins, including 14-3-3 isoforms, that bind O-GlcNAc directly and selectively. We demonstrate that 14-3-3 proteins bind O-GlcNAc moieties in human cells, and we present the structures of 14-3-3beta/alpha and gamma bound to glycopeptides, providing biophysical insights into O-GlcNAc-mediated protein-protein interactions. Because 14-3-3 proteins also bind to phospho-serine and phospho-threonine, they may integrate information from O-GlcNAc and O-phosphate signaling pathways to regulate numerous physiological functions.
Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins.,Toleman CA, Schumacher MA, Yu SH, Zeng W, Cox NJ, Smith TJ, Soderblom EJ, Wands AM, Kohler JJ, Boyce M Proc Natl Acad Sci U S A. 2018 May 21. pii: 1722437115. doi:, 10.1073/pnas.1722437115. PMID:29784830[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jin Y, Dai MS, Lu SZ, Xu Y, Luo Z, Zhao Y, Lu H. 14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation. EMBO J. 2006 Mar 22;25(6):1207-18. Epub 2006 Mar 2. PMID:16511572 doi:10.1038/sj.emboj.7601010
- ↑ Toleman CA, Schumacher MA, Yu SH, Zeng W, Cox NJ, Smith TJ, Soderblom EJ, Wands AM, Kohler JJ, Boyce M. Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins. Proc Natl Acad Sci U S A. 2018 May 21. pii: 1722437115. doi:, 10.1073/pnas.1722437115. PMID:29784830 doi:http://dx.doi.org/10.1073/pnas.1722437115
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