4MNG
Structure of the DP10.7 TCR with CD1d-sulfatide
Summary for 4MNG
Entry DOI | 10.2210/pdb4mng/pdb |
Descriptor | Beta-2-microglobulin, Cd1d1 protein, TRA@ protein,TRA@ protein, Ti antigen CD3-associated protein gamma chain V-J-C region, ... (6 entities in total) |
Functional Keywords | immunglobulin, histocompatibility antigens, cd1, immunological, lymphocytes, gamma delta t cell, t cell recognition, self-recognition, myelin, intestinal epithelial lymphocytes, human, lipid binding, self-ligand, glycoproteins, cell-surface receptors, immune system |
Biological source | Mus musculus (Mouse) More |
Total number of polymer chains | 6 |
Total formula weight | 147443.98 |
Authors | Luoma, A.M.,Adams, E.J. (deposition date: 2013-09-10, release date: 2013-12-18, Last modification date: 2024-10-30) |
Primary citation | Luoma, A.M.,Castro, C.D.,Mayassi, T.,Bembinster, L.A.,Bai, L.,Picard, D.,Anderson, B.,Scharf, L.,Kung, J.E.,Sibener, L.V.,Savage, P.B.,Jabri, B.,Bendelac, A.,Adams, E.J. Crystal Structure of V delta 1 T Cell Receptor in Complex with CD1d-Sulfatide Shows MHC-like Recognition of a Self-Lipid by Human gamma delta T Cells. Immunity, 39:1032-1042, 2013 Cited by PubMed Abstract: The nature of the antigens recognized by γδ T cells and their potential recognition of major histocompatibility complex (MHC)-like molecules has remained unclear. Members of the CD1 family of lipid-presenting molecules are suggested ligands for Vδ1 TCR-expressing γδ T cells, the major γδ lymphocyte population in epithelial tissues. We crystallized a Vδ1 TCR in complex with CD1d and the self-lipid sulfatide, revealing the unusual recognition of CD1d by germline Vδ1 residues spanning all complementarity-determining region (CDR) loops, as well as sulfatide recognition separately encoded by nongermline CDR3δ residues. Binding and functional analysis showed that CD1d presenting self-lipids, including sulfatide, was widely recognized by gut Vδ1+ γδ T cells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by γδ T cells and reveal the prevalence of lipid recognition by innate-like T cell populations. PubMed: 24239091DOI: 10.1016/j.immuni.2013.11.001 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.0058 Å) |
Structure validation
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