4PG2
The crystal structure of H-2Db with a S-glutathionylated peptide
4PG2 の概要
| エントリーDOI | 10.2210/pdb4pg2/pdb |
| 分子名称 | H-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, CYS-SER-LEU-TRP-ASN-GLY-PRO-HIS-LEU, ... (6 entities in total) |
| 機能のキーワード | immune receptor, glutathionylated peptide, t cell biology, antigen presentation, immune system |
| 由来する生物種 | Mus musculus (Mouse) 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 45500.89 |
| 構造登録者 | |
| 主引用文献 | Trujillo, J.A.,Croft, N.P.,Dudek, N.L.,Channappanavar, R.,Theodossis, A.,Webb, A.I.,Dunstone, M.A.,Illing, P.T.,Butler, N.S.,Fett, C.,Tscharke, D.C.,Rossjohn, J.,Perlman, S.,Purcell, A.W. The cellular redox environment alters antigen presentation. J.Biol.Chem., 289:27979-27991, 2014 Cited by PubMed Abstract: 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. PubMed: 25135637DOI: 10.1074/jbc.M114.573402 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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