6mwr

Recognition of MHC-like molecule

spinqualitylabelsall models 6mwr, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mwr is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3Å Ligands: 2LJ, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HMR1_HUMAN Has antigen presentation function. Involved in the development and expansion of a small population of T-cells expressing an invariant T-cell receptor alpha chain called mucosal-associated invariant T-cells (MAIT). MAIT cells are preferentially located in the gut lamina propria and therefore may be involved in monitoring commensal flora or serve as a distress signal. Expression and MAIT cell recognition seem to be ligand-dependent. Publication Abstract from PubMed 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 gammadelta T cells isolated from peripheral blood and tissues that exhibit autoreactivity to the monomorphic MHC-related protein 1 (MR1). The crystal structure of a gammadeltaTCR-MR1-antigen complex starkly contrasts with all other TCR-MHC and TCR-MHC-I-like complex structures. Namely, the gammadeltaTCR binds underneath the MR1 antigen-binding cleft, where contacts are dominated by the MR1 alpha3 domain. A similar pattern of reactivity was observed for diverse MR1-restricted gammadeltaTCRs from multiple individuals. Accordingly, we simultaneously report MR1 as a ligand for human gammadelta T cells and redefine the parameters for TCR recognition. A class of gammadelta T cell receptors recognize the underside of the antigen-presenting molecule MR1.,Le Nours J, Gherardin NA, Ramarathinam SH, Awad W, Wiede F, Gully BS, Khandokar Y, Praveena T, Wubben JM, Sandow JJ, Webb AI, von Borstel A, Rice MT, Redmond SJ, Seneviratna R, Sandoval-Romero ML, Li S, Souter MNT, Eckle SBG, Corbett AJ, Reid HH, Liu L, Fairlie DP, Giles EM, Westall GP, Tothill RW, Davey MS, Berry R, Tiganis T, McCluskey J, Pellicci DG, Purcell AW, Uldrich AP, Godfrey DI, Rossjohn J Science. 2019 Dec 20;366(6472):1522-1527. doi: 10.1126/science.aav3900. PMID:31857486 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures T-cell receptor 3D structures

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