8TQA

Crystal structure of Fab.28.14.8 in complex with MHC-I (H2-Db)

8TQA の概要

• エントリーDOI: 10.2210/pdb8tqa/pdb
• 関連するPDBエントリー: 8TQ4 8TQ5 8TQ6 8TQ7 8TQ8 8TQ9
• 分子名称: H-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, Fab.28.14S Heavy chain, ... (9 entities in total)
• 機能のキーワード: histocompatibility complex class i, mhc-i, immune response, immune system fab, antibody, anti-mhc antibody, cancer tumor, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 92570.07

構造登録者

Jiang, J.,Boyd, L.F.,Natarajan, K.,Margulies, D.H. (登録日: 2023-08-06, 公開日: 2024-03-20, 最終更新日: 2024-10-16)

主引用文献

Boyd, L.F.,Jiang, J.,Ahmad, J.,Natarajan, K.,Margulies, D.H.
Experimental Structures of Antibody/MHC-I Complexes Reveal Details of Epitopes Overlooked by Computational Prediction.
J Immunol., 212:1366-1380, 2024

PubMed Abstract: mAbs to MHC class I (MHC-I) molecules have proved to be crucial reagents for tissue typing and fundamental studies of immune recognition. To augment our understanding of epitopic sites seen by a set of anti-MHC-I mAb, we determined X-ray crystal structures of four complexes of anti-MHC-I Fabs bound to peptide/MHC-I/β2-microglobulin (pMHC-I). An anti-H2-Dd mAb, two anti-MHC-I α3 domain mAbs, and an anti-β2-microglobulin mAb bind pMHC-I at sites consistent with earlier mutational and functional experiments, and the structures explain allelomorph specificity. Comparison of the experimentally determined structures with computationally derived models using AlphaFold Multimer showed that although predictions of the individual pMHC-I heterodimers were quite acceptable, the computational models failed to properly identify the docking sites of the mAb on pMHC-I. The experimental and predicted structures provide insight into strengths and weaknesses of purely computational approaches and suggest areas that merit additional attention.

PubMed: 38456672
DOI: 10.4049/jimmunol.2300839

実験手法

X-RAY DIFFRACTION (2.6 Å)