7CIS
Peptide modification of MHC class I molecules
7CIS の概要
| エントリーDOI | 10.2210/pdb7cis/pdb |
| 分子名称 | MHC class I antigen, Beta-2-microglobulin, ARG-ARG-PHE-SEP-ARG-SEP-PRO-ILE-ARG, ... (4 entities in total) |
| 機能のキーワード | mhc i complex, dip-son3-9, immune system |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 45145.87 |
| 構造登録者 | |
| 主引用文献 | Zhao, Y.,Sun, M.,Zhang, N.,Liu, X.,Yue, C.,Feng, L.,Ji, S.,Liu, X.,Qi, J.,Wong, C.C.L.,Gao, G.F.,Liu, W.J. Phosphosite-dependent presentation of dual phosphorylated peptides by MHC class I molecules. Iscience, 25:104013-104013, 2022 Cited by PubMed Abstract: Phosphopeptides presented by major histocompatibility complex (MHC) class I have been regarded as a pivotal type of cancer neoantigens that are recognized by T cells. The structural basis of single-phosphorylated peptide presentation has been well studied. Diphosphorylation with one interval between two sites is one of the prevalent forms of multisite-phosphorylated peptides. Herein, we determined the molecular basis of presentation of two P4/P6 double pS-containing peptides by HLA-B27 and compared them with unmodified and single-phosphorylated peptide complexes. These data clarified not only the HLA allele-specific presentation of phosphopeptides by MHC class I molecules but also the cooperativity of peptide conformation within P4 and P6 phosphorylation sites. The phosphorylation of P6 site can influence the binding mode of P4 phosphorylated site to HLA-B27. And we found the diphospho-dependent attenuated effect of peptide binding affinity. This study provides insights into the MHC presentation features of diphosphopeptides, which is different from monophosphopeptides. PubMed: 35310951DOI: 10.1016/j.isci.2022.104013 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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