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7S8I

PHOSPHOPEPTIDE-SPECIFIC LC13 TCR, MONOCLINIC CRYSTAL FORM

7S8I の概要
エントリーDOI10.2210/pdb7s8i/pdb
分子名称TRAV27_LC13 TCR ALPHA CHAIN, TRBV27_LC13 TCR BETA CHAIN, CHLORIDE ION, ... (4 entities in total)
機能のキーワードhla, mll peptide, hla-b*07:02, hla-b7, immunity, immune system, phosphopeptide, cancer, neoantigen, tcr
由来する生物種Homo sapiens (HUMAN)
詳細
タンパク質・核酸の鎖数2
化学式量合計50331.62
構造登録者
主引用文献Patskovsky, Y.,Natarajan, A.,Patskovska, L.,Nyovanie, S.,Joshi, B.,Morin, B.,Brittsan, C.,Huber, O.,Gordon, S.,Michelet, X.,Schmitzberger, F.,Stein, R.B.,Findeis, M.A.,Hurwitz, A.,Van Dijk, M.,Chantzoura, E.,Yague, A.S.,Pollack Smith, D.,Buell, J.S.,Underwood, D.,Krogsgaard, M.
Molecular mechanism of phosphopeptide neoantigen immunogenicity.
Nat Commun, 14:3763-3763, 2023
Cited by
PubMed Abstract: Altered protein phosphorylation in cancer cells often leads to surface presentation of phosphopeptide neoantigens. However, their role in cancer immunogenicity remains unclear. Here we describe a mechanism by which an HLA-B*0702-specific acute myeloid leukemia phosphoneoantigen, pMLL (EPR(pS)PSHSM), is recognized by a cognate T cell receptor named TCR27, a candidate for cancer immunotherapy. We show that the replacement of phosphoserine P with serine or phosphomimetics does not affect pMHC conformation or peptide-MHC affinity but abrogates TCR27-dependent T cell activation and weakens binding between TCR27 and pMHC. Here we describe the crystal structures for TCR27 and cognate pMHC, map of the interface produced by nuclear magnetic resonance, and a ternary complex generated using information-driven protein docking. Our data show that non-covalent interactions between the epitope phosphate group and TCR27 are crucial for TCR specificity. This study supports development of new treatment options for cancer patients through target expansion and TCR optimization.
PubMed: 37353482
DOI: 10.1038/s41467-023-39425-1
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.66 Å)
構造検証レポート
Validation report summary of 7s8i
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2026-02-04に公開中

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