3QIU

Crystal structure of the 226 TCR in complex with MCC/I-Ek

3QIU の概要

• エントリーDOI: 10.2210/pdb3qiu/pdb
• 分子名称: H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, E-K alpha chain, MHC CLASS II H2-IA-BETA CHAIN, TCR 226 alpha chain, ... (7 entities in total)
• 機能のキーワード: immunoglobulin domain, t cell receptor, mhc molecule, immune system
• 由来する生物種: Mus musculus (mouse); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 96078.13

構造登録者

Kruse, A.C.,Ely, L.K.,Newell, E.W.,Davis, M.M.,Garcia, K.C. (登録日: 2011-01-27, 公開日: 2011-04-27, 最終更新日: 2024-11-27)

主引用文献

Newell, E.W.,Ely, L.K.,Kruse, A.C.,Reay, P.A.,Rodriguez, S.N.,Lin, A.E.,Kuhns, M.S.,Garcia, K.C.,Davis, M.M.
Structural basis of specificity and cross-reactivity in T cell receptors specific for cytochrome c-I-E(k).
J.Immunol., 186:5823-5832, 2011

PubMed Abstract: T cells specific for the cytochrome c Ag are widely used to investigate many aspects of TCR specificity and interactions with peptide-MHC, but structural information has long been elusive. In this study, we present structures for the well-studied 2B4 TCR, as well as a naturally occurring variant of the 5c.c7 TCR, 226, which is cross-reactive with more than half of possible substitutions at all three TCR-sensitive residues on the peptide Ag. These structures alone and in complex with peptide-MHC ligands allow us to reassess many prior mutagenesis results. In addition, the structure of 226 bound to one peptide variant, p5E, shows major changes in the CDR3 contacts compared with wild-type, yet the TCR V-region contacts with MHC are conserved. These and other data illustrate the ability of TCRs to accommodate large variations in CDR3 structure and peptide contacts within the constraints of highly conserved TCR-MHC interactions.

PubMed: 21490152
DOI: 10.4049/jimmunol.1100197

実験手法

X-RAY DIFFRACTION (2.7 Å)