4P2R

Crystal structure of the 5cc7 TCR in complex with 5c1/I-Ek

Summary for 4P2R

• Entry DOI: 10.2210/pdb4p2r/pdb
• Related: 4P2O 4P2Q
• Descriptor: H-2 class II histocompatibility antigen, E-K alpha chain, MHC class II E-beta-k, 5c1 peptide, ... (6 entities in total)
• Functional Keywords: t cell receptor, peptide-mhc complex, immune system
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 20
• Total formula weight: 408348.00

Authors

Birnbaum, M.E.,Ozkan, E.,Garcia, K.C. (deposition date: 2014-03-04, release date: 2014-05-21, Last modification date: 2023-12-27)

Primary citation

Birnbaum, M.E.,Mendoza, J.L.,Sethi, D.K.,Dong, S.,Glanville, J.,Dobbins, J.,Ozkan, E.,Davis, M.M.,Wucherpfennig, K.W.,Garcia, K.C.
Deconstructing the Peptide-MHC Specificity of T Cell Recognition.
Cell, 157:1073-1087, 2014

PubMed Abstract: In order to survey a universe of major histocompatibility complex (MHC)-presented peptide antigens whose numbers greatly exceed the diversity of the T cell repertoire, T cell receptors (TCRs) are thought to be cross-reactive. However, the nature and extent of TCR cross-reactivity has not been conclusively measured experimentally. We developed a system to identify MHC-presented peptide ligands by combining TCR selection of highly diverse yeast-displayed peptide-MHC libraries with deep sequencing. Although we identified hundreds of peptides reactive with each of five different mouse and human TCRs, the selected peptides possessed TCR recognition motifs that bore a close resemblance to their known antigens. This structural conservation of the TCR interaction surface allowed us to exploit deep-sequencing information to computationally identify activating microbial and self-ligands for human autoimmune TCRs. The mechanistic basis of TCR cross-reactivity described here enables effective surveillance of diverse self and foreign antigens without necessitating degenerate recognition of nonhomologous peptides.

PubMed: 24855945
DOI: 10.1016/j.cell.2014.03.047

Experimental method

X-RAY DIFFRACTION (3.295 Å)