5sws
Crystal Structure of NP2-B17 TCR-H2Db-NP complexCrystal Structure of NP2-B17 TCR-H2Db-NP complex
Structural highlights
Function[HA11_MOUSE] Involved in the presentation of foreign antigens to the immune system. [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Publication Abstract from PubMedThe anti-viral T cell response is drawn from the naive T cell repertoire. During influenza infection, the CD8+ T cell response to an H-2Db-restricted nucleoprotein epitope (NP366) is characterized by preferential expansion of T cells bearing TRBV13+ T cell receptors (TCRs) and avoidance of TRBV17+ T cells, despite the latter dominating the naive precursor repertoire. We found two TRBV17+ TCRs that bound H-2Db-NP366 with a 180 degrees reversed polarity compared to the canonical TCR-pMHC-I docking. The TRBV17 beta-chain dominated the interaction and, whereas the complementarity determining region-3 (CDR3) loops exclusively mediated contacts with the MHC-I, peptide specificity was attributable to germline-encoded recognition. Nevertheless, the TRBV17+ TCR exhibited moderate affinity toward H-2Db-NP366 and was capable of signal transduction. Thus, the naive CD8+ T cell pool can comprise TCRs adopting reversed pMHC-I docking modes that limit their involvement in the immune response. Reversed T Cell Receptor Docking on a Major Histocompatibility Class I Complex Limits Involvement in the Immune Response.,Gras S, Chadderton J, Del Campo CM, Farenc C, Wiede F, Josephs TM, Sng XY, Mirams M, Watson KA, Tiganis T, Quinn KM, Rossjohn J, La Gruta NL Immunity. 2016 Oct 18;45(4):749-760. doi: 10.1016/j.immuni.2016.09.007. Epub 2016, Oct 4. PMID:27717799[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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