6MWR
Recognition of MHC-like molecule
Summary for 6MWR
| Entry DOI | 10.2210/pdb6mwr/pdb |
| Descriptor | Major histocompatibility complex class I-related gene protein, Beta-2-microglobulin, G7 Gamma chain T cell receptor, ... (7 entities in total) |
| Functional Keywords | mhc-like molecule, immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 98139.13 |
| Authors | Le Nours, J.,Rossjohn, J. (deposition date: 2018-10-30, release date: 2019-12-18, Last modification date: 2024-10-23) |
| Primary citation | Le Nours, J.,Gherardin, N.A.,Ramarathinam, S.H.,Awad, W.,Wiede, F.,Gully, B.S.,Khandokar, Y.,Praveena, T.,Wubben, J.M.,Sandow, J.J.,Webb, A.I.,von Borstel, A.,Rice, M.T.,Redmond, S.J.,Seneviratna, R.,Sandoval-Romero, M.L.,Li, S.,Souter, M.N.T.,Eckle, S.B.G.,Corbett, A.J.,Reid, H.H.,Liu, L.,Fairlie, D.P.,Giles, E.M.,Westall, G.P.,Tothill, R.W.,Davey, M.S.,Berry, R.,Tiganis, T.,McCluskey, J.,Pellicci, D.G.,Purcell, A.W.,Uldrich, A.P.,Godfrey, D.I.,Rossjohn, J. A class of gamma delta T cell receptors recognize the underside of the antigen-presenting molecule MR1. Science, 366:1522-1527, 2019 Cited by PubMed Abstract: T cell receptors (TCRs) recognize antigens presented by major histocompatibility complex (MHC) and MHC class I-like molecules. We describe a diverse population of human γδ T cells isolated from peripheral blood and tissues that exhibit autoreactivity to the monomorphic MHC-related protein 1 (MR1). The crystal structure of a γδTCR-MR1-antigen complex starkly contrasts with all other TCR-MHC and TCR-MHC-I-like complex structures. Namely, the γδTCR binds underneath the MR1 antigen-binding cleft, where contacts are dominated by the MR1 α3 domain. A similar pattern of reactivity was observed for diverse MR1-restricted γδTCRs from multiple individuals. Accordingly, we simultaneously report MR1 as a ligand for human γδ T cells and redefine the parameters for TCR recognition. PubMed: 31857486DOI: 10.1126/science.aav3900 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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