1EEY

Crystal Structure Determination Of HLA A2 Complexed to Peptide GP2 with the substitution (I2L/V5L/L9V)

1EEY の概要

• エントリーDOI: 10.2210/pdb1eey/pdb
• 関連するPDBエントリー: 1EEZ 1QR1
• 分子名称: HLA-A2.1 MHC CLASS I (HEAVY CHAIN), BETA-2-MICROGLOBULIN (LIGHT CHAIN), GP2 PEPTIDE, ... (4 entities in total)
• 機能のキーワード: major histicompatibility complex, peptide binding, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01892; Secreted: P01884
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 89235.35

構造登録者

Sharma, A.K.,Kuhns, J.J.,Collins, E.J. (登録日: 2000-02-04, 公開日: 2003-06-10, 最終更新日: 2024-10-16)

主引用文献

Sharma, A.K.,Kuhns, J.J.,Yan, S.,Friedline, R.H.,Long, B.,Tisch, R.,Collins, E.J.
Class I major histocompatibility complex anchor substitutions alter the conformation of T cell receptor contacts.
J.Biol.Chem., 276:21443-21449, 2001

PubMed Abstract: An immunogenic peptide (GP2) derived from HER-2/neu binds to HLA-A2.1 very poorly. Some altered-peptide ligands (APL) of GP2 have increased binding affinity and generate improved cytotoxic T lymphocyte recognition of GP2-presenting tumor cells, but most do not. Increases in binding affinity of single-substitution APL are not additive in double-substitution APL. A common first assumption about peptide binding to class I major histocompatibility complex is that each residue binds independently. In addition, immunologists interested in immunotherapy frequently assume that anchor substitutions do not affect T cell receptor contact residues. However, the crystal structures of two GP2 APL show that the central residues change position depending on the identity of the anchor residue(s). Thus, it is clear that subtle changes in the identity of anchor residues may have significant effects on the positions of the T cell receptor contact residues.

PubMed: 11287414
DOI: 10.1074/jbc.M010791200

実験手法

X-RAY DIFFRACTION (2.25 Å)