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7CIS

Peptide modification of MHC class I molecules

7CIS の概要
エントリーDOI10.2210/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
Sun, M.W.,Feng, L.,Qi, J.X.,Liu, W.J.,Gao, G.F. (登録日: 2020-07-08, 公開日: 2022-03-09, 最終更新日: 2024-11-06)
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: 35310951
DOI: 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)
構造検証レポート
Validation report summary of 7cis
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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