3QJF

Crystal structure of the 2B4 TCR

Summary for 3QJF

• Entry DOI: 10.2210/pdb3qjf/pdb
• Related: 3QIB 3QIW 3QJH
• Descriptor: 2B4 alpha chain, 2B4 beta chain (3 entities in total)
• Functional Keywords: immunoglobulin domain, t cell receptor, immune system
• Biological source: Mus musculus; More
• Total number of polymer chains: 4
• Total formula weight: 101322.68

Authors

Ely, L.K.,Newell, E.W.,Davis, M.M.,Garcia, K.C. (deposition date: 2011-01-28, release date: 2011-04-27, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)