5WLI
Crystal Structure of H-2Db with the GAP501 peptide (SQL)
Summary for 5WLI
| Entry DOI | 10.2210/pdb5wli/pdb |
| Related | 5wlg |
| Descriptor | H-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, GAP50 peptide, ... (5 entities in total) |
| Functional Keywords | h-2db, malaria, gap50, immune response gene, tcr, t cell, vb8.1, immune system |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 12 |
| Total formula weight | 180254.95 |
| Authors | Gras, S.,Farenc, C.,Josephs, T.,Rossjohn, J. (deposition date: 2017-07-27, release date: 2017-11-15, Last modification date: 2024-11-06) |
| Primary citation | Van Braeckel-Budimir, N.,Gras, S.,Ladell, K.,Josephs, T.M.,Pewe, L.,Urban, S.L.,Miners, K.L.,Farenc, C.,Price, D.A.,Rossjohn, J.,Harty, J.T. A T Cell Receptor Locus Harbors a Malaria-Specific Immune Response Gene. Immunity, 47:835-847.e4, 2017 Cited by PubMed Abstract: Immune response (Ir) genes, originally proposed by Baruj Benacerraf to explain differential antigen-specific responses in animal models, have become synonymous with the major histocompatibility complex (MHC). We discovered a non-MHC-linked Ir gene in a T cell receptor (TCR) locus that was required for CD8 T cell responses to the Plasmodium berghei GAP50 epitope in mice expressing the MHC class I allele H-2D. GAP50-specific CD8 T cell responses emerged from a very large pool of naive Vβ8.1 precursors, which dictated susceptibility to cerebral malaria and conferred protection against recombinant Listeria monocytogenes infection. Structural analysis of a prototypical Vβ8.1 TCR-H-2D-GAP50 ternary complex revealed that germline-encoded complementarity-determining region 1β residues present exclusively in the Vβ8.1 segment mediated essential interactions with the GAP50 peptide. Collectively, these findings demonstrated that Vβ8.1 functioned as an Ir gene that was indispensable for immune reactivity against the malaria GAP50 epitope. PubMed: 29150238DOI: 10.1016/j.immuni.2017.10.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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