4pg2
From Proteopedia
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- | '''Unreleased structure''' | ||
- | The | + | ==The crystal structure of H-2Db with a S-glutathionylated peptide== |
+ | <StructureSection load='4pg2' size='340' side='right'caption='[[4pg2]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4pg2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=4PG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PG2 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4pg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pg2 OCA], [https://pdbe.org/4pg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pg2 RCSB], [https://www.ebi.ac.uk/pdbsum/4pg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pg2 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/HA11_MOUSE HA11_MOUSE] Involved in the presentation of foreign antigens to the immune system. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Cysteine-containing peptides represent an important class of T cell epitopes, yet their prevalence remains underestimated. We have established and interrogated a database of around 70,000 naturally processed MHC bound peptides and demonstrate that cysteine-containing peptides are presented on the surface of cells in an MHC allomorph dependent manner and comprise on average 5-10% of the immunopeptidome. A significant proportion of these peptides are oxidatively modified, most commonly through covalent linkage with the antioxidant glutathione. Unlike some of the previously reported Cysteine-based modifications, this represents a true physiological alteration of cysteine residues. Furthermore, our results suggest that alterations in the cellular redox state induced by viral infection are communicated to the immune system through the presentation of S-glutathionylated viral peptides, resulting in altered T cell recognition. Our data provide a structural basis for how the glutathione modification alters recognition by virus-specific T cells. Collectively, these results suggest that oxidative stress represents a mechanism for modulating the virus-specific T cell response. | ||
- | + | The Cellular Redox Environment Alters Antigen Presentation.,Trujillo JA, Croft NP, Dudek NL, Channappanavar R, Theodossis A, Webb AI, Dunstone MA, Illing PT, Butler NS, Fett C, Tscharke DC, Rossjohn J, Perlman S, Purcell AW J Biol Chem. 2014 Aug 18. pii: jbc.M114.573402. PMID:25135637<ref>PMID:25135637</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 4pg2" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Mus musculus]] | ||
+ | [[Category: Synthetic construct]] | ||
+ | [[Category: Rossjohn J]] | ||
+ | [[Category: Theodossis A]] |
Current revision
The crystal structure of H-2Db with a S-glutathionylated peptide
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