5L2J
Crystal Structure of human CD1b in complex with C36-GMM
Summary for 5L2J
Entry DOI | 10.2210/pdb5l2j/pdb |
Related | 5L2K |
Descriptor | T-cell surface glycoprotein CD1b, Beta-2-microglobulin, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
Functional Keywords | cd1b, lipid, tb, mtb, gmm, tuberculosis, gem t cell, tcr, t cell, immune system |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 48092.11 |
Authors | Gras, S.,Shahine, A.,Le Nours, J.,Rossjohn, J. (deposition date: 2016-08-02, release date: 2016-11-16, Last modification date: 2024-11-20) |
Primary citation | Gras, S.,Van Rhijn, I.,Shahine, A.,Cheng, T.Y.,Bhati, M.,Tan, L.L.,Halim, H.,Tuttle, K.D.,Gapin, L.,Le Nours, J.,Moody, D.B.,Rossjohn, J. T cell receptor recognition of CD1b presenting a mycobacterial glycolipid. Nat Commun, 7:13257-13257, 2016 Cited by PubMed Abstract: CD1 proteins present microbial lipids to T cells. Germline-encoded mycolyl lipid-reactive (GEM) T cells with conserved αβ T cell receptors (TCRs) recognize CD1b presenting mycobacterial mycolates. As the molecular basis underpinning TCR recognition of CD1b remains unknown, here we determine the structure of a GEM TCR bound to CD1b presenting glucose-6-O-monomycolate (GMM). The GEM TCR docks centrally above CD1b, whereby the conserved TCR α-chain extensively contacts CD1b and GMM. Through mutagenesis and study of T cells from tuberculosis patients, we identify a consensus CD1b footprint of TCRs present among GEM T cells. Using both the TCR α- and β-chains as tweezers to surround and grip the glucose moiety of GMM, GEM TCRs create a highly specific mechanism for recognizing this mycobacterial glycolipid. PubMed: 27807341DOI: 10.1038/ncomms13257 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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