6XNG
MHC-like protein complex structure
Summary for 6XNG
| Entry DOI | 10.2210/pdb6xng/pdb |
| Descriptor | Antigen-presenting glycoprotein CD1d1, Beta-2-microglobulin, NKT Valpha14 (Mouse)-2C12 TCR, ... (8 entities in total) |
| Functional Keywords | mhc-like protein, cd1d1 antigen presenting molecule, lipid binding protein complex, lipid binding protein |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 99086.98 |
| Authors | Thirunavukkarasu, P.,Le Nours, J.,Rossjohn, J. (deposition date: 2020-07-02, release date: 2021-11-10, Last modification date: 2024-11-06) |
| Primary citation | Oh, S.F.,Praveena, T.,Song, H.,Yoo, J.S.,Jung, D.J.,Erturk-Hasdemir, D.,Hwang, Y.S.,Lee, C.C.,Le Nours, J.,Kim, H.,Lee, J.,Blumberg, R.S.,Rossjohn, J.,Park, S.B.,Kasper, D.L. Host immunomodulatory lipids created by symbionts from dietary amino acids. Nature, 600:302-307, 2021 Cited by PubMed Abstract: Small molecules derived from symbiotic microbiota critically contribute to intestinal immune maturation and regulation. However, little is known about the molecular mechanisms that control immune development in the host-microbiota environment. Here, using a targeted lipidomic analysis and synthetic approach, we carried out a multifaceted investigation of immunomodulatory α-galactosylceramides from the human symbiont Bacteroides fragilis (BfaGCs). The characteristic terminal branching of BfaGCs is the result of incorporation of branched-chain amino acids taken up in the host gut by B. fragilis. A B. fragilis knockout strain that cannot metabolize branched-chain amino acids showed reduced branching in BfaGCs, and mice monocolonized with this mutant strain had impaired colonic natural killer T (NKT) cell regulation, implying structure-specific immunomodulatory activity. The sphinganine chain branching of BfaGCs is a critical determinant of NKT cell activation, which induces specific immunomodulatory gene expression signatures and effector functions. Co-crystal structure and affinity analyses of CD1d-BfaGC-NKT cell receptor complexes confirmed the interaction of BfaGCs as CD1d-restricted ligands. We present a structural and molecular-level paradigm of immunomodulatory control by interactions of endobiotic metabolites with diet, microbiota and the immune system. PubMed: 34759313DOI: 10.1038/s41586-021-04083-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
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