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5SWZ

Crystal Structure of NP1-B17 TCR-H2Db-NP complex

Summary for 5SWZ
Entry DOI10.2210/pdb5swz/pdb
Related5SWS
DescriptorH-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, influenza NP366 epitope, ... (8 entities in total)
Functional Keywordsh2db, influenza, np366, reversed docking, naive t cell, np1-b17 tcr, tcr, t cell, immune system
Biological sourceMus musculus (Mouse)
More
Cellular locationMembrane; Single-pass type I membrane protein: P01899
Secreted: P01887
Total number of polymer chains20
Total formula weight385186.72
Authors
Gras, S.,Del Campo, C.M.,Farenc, C.,Josephs, T.M.,Rossjohn, J. (deposition date: 2016-08-09, release date: 2016-10-05, Last modification date: 2024-10-16)
Primary citationGras, S.,Chadderton, J.,Del Campo, C.M.,Farenc, C.,Wiede, F.,Josephs, T.M.,Sng, X.Y.,Mirams, M.,Watson, K.A.,Tiganis, T.,Quinn, K.M.,Rossjohn, J.,La Gruta, N.L.
Reversed T Cell Receptor Docking on a Major Histocompatibility Class I Complex Limits Involvement in the Immune Response.
Immunity, 45:749-760, 2016
Cited by
PubMed Abstract: The anti-viral T cell response is drawn from the naive T cell repertoire. During influenza infection, the CD8 T cell response to an H-2D-restricted nucleoprotein epitope (NP) 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-2D-NP with a 180° reversed polarity compared to the canonical TCR-pMHC-I docking. The TRBV17 β-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-2D-NP 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.
PubMed: 27717799
DOI: 10.1016/j.immuni.2016.09.007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

227344

数据于2024-11-13公开中

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