6byl
From Proteopedia
(Difference between revisions)
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==Structure of 14-3-3 gamma bound to O-GlcNAcylated thr peptide== | ==Structure of 14-3-3 gamma bound to O-GlcNAcylated thr peptide== | ||
| - | <StructureSection load='6byl' size='340' side='right' caption='[[6byl]], [[Resolution|resolution]] 3.35Å' scene=''> | + | <StructureSection load='6byl' size='340' side='right'caption='[[6byl]], [[Resolution|resolution]] 3.35Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6byl]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BYL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6byl]] is a 9 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=6BYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BYL 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6byl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6byl OCA], [http://pdbe.org/6byl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6byl RCSB], [http://www.ebi.ac.uk/pdbsum/6byl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6byl 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=6byl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6byl OCA], [http://pdbe.org/6byl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6byl RCSB], [http://www.ebi.ac.uk/pdbsum/6byl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6byl 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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:29784830</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6byl" style="background-color:#fffaf0;"></div> | ||
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| + | ==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: Large Structures]] | ||
[[Category: Schumacher, M A]] | [[Category: Schumacher, M A]] | ||
[[Category: 14-3-3]] | [[Category: 14-3-3]] | ||
[[Category: O-glcnac]] | [[Category: O-glcnac]] | ||
[[Category: Peptide binding protein]] | [[Category: Peptide binding protein]] | ||
Revision as of 07:27, 23 May 2019
Structure of 14-3-3 gamma bound to O-GlcNAcylated thr peptide
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