1KBG

MHC Class I H-2KB Presented Glycopeptide RGY8-6H-GAL2

1KBG の概要

• エントリーDOI: 10.2210/pdb1kbg/pdb
• 分子名称: PROTEIN (MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I ANTIGEN H-2KB), PROTEIN (BETA-2-MICROGLOBULIN), PROTEIN (SYNTHETIC GLYCOPEPTIDE RGY8-6H-GAL2), ... (7 entities in total)
• 機能のキーワード: mhc, major histocompatibility complex, antigen presentation, glycopeptide, cellular immunity, immunology, cell surface receptor, synthetic peptide, vaccine, 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: 3
• 化学式量合計: 45459.90

構造登録者

Speir, J.A.,Abdel-Motal, U.M.,Jondal, M.,Wilson, I.A. (登録日: 1998-08-28, 公開日: 1999-02-09, 最終更新日: 2023-11-15)

主引用文献

Speir, J.A.,Abdel-Motal, U.M.,Jondal, M.,Wilson, I.A.
Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL.
Immunity, 10:51-61, 1999

PubMed Abstract: T cell receptor (TCR) recognition of nonpeptidic and modified peptide antigens has been recently uncovered but is still poorly understood. Immunization with an H-2Kb-restricted glycopeptide RGY8-6H-Gal2 generates a population of cytotoxic T cells that express both alpha/beta TCR, specific for glycopeptide, and gamma/delta TCR, specific for the disaccharide, even on glycolipids. The crystal structure of Kb/RGY8-6H-Gal2 now demonstrates that the peptide and H-2Kb structures are unaffected by the peptide glycosylation, but the central region of the putative TCR binding site is dominated by the extensive exposure of the tethered carbohydrate. These features of the Kb/RGY8-6H-Gal2 structure are consistent with the individual ligand binding preferences identified for the alpha/beta and gamma/delta TCRs and thus explain the generation of a carbohydrate-specific T cell response.

PubMed: 10023770
DOI: 10.1016/S1074-7613(00)80006-0

実験手法

X-RAY DIFFRACTION (2.2 Å)