26sk | pdb_000026sk

Crystal structure of MAIT A-F7 TCR-MR1-uric acid

spinqualitylabelsall models 26sk, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 26sk is a 8 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 2.85Å Ligands: ACT, CA, CL, GOL, URC 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 The major histocompatibility complex class I-related molecule (MR1) is a non-classical antigen-presenting protein that presents a diverse array of microbial, synthetic and host-generated small metabolites to mucosal-associated invariant T (MAIT) cells and other MR1-restricted T (MR1T) cell populations. Recent studies showed that MR1 binds carbonyl-nucleobase adducts, resulting in the activation of some MR1T cell clones. However, whether endogenous canonical nucleobases and their derivatives can impact the MR1 axis remains unclear. Here, through biochemical and cellular screening of a library of canonical nucleobases and their catabolites, we demonstrate that the catabolites of purine degradation, namely uric acid, xanthine, and xanthosine, can, at high concentrations, bind MR1 and promote its intracellular retention, resulting in reduced MR1 surface expression. These purine-based nucleobases can compete with microbial and non-microbial ligands for MR1 binding. Analysis of three crystal structures of ligand-bound MR1 shows that these endogenous purine-based nucleobases adopt distinct modes of binding and interactions within the MR1 A'-pocket. Accordingly, we broaden the repertoire of MR1-ligandome by describing a group of host xanthine-based compounds that can bind MR1 and regulate its trafficking to the cell surface. The MHC-I related protein 1 MR1 can bind host purine catabolites.,Abdelaal MR, Lim XY, Mak JYW, Fairlie DP, McCluskey J, Corbett AJ, Gherardin NA, Awad W, Rossjohn J J Biol Chem. 2026 Aug 12;302(10):113428. doi: 10.1016/j.jbc.2026.113428. PMID:42586424 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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