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5L2J

Crystal Structure of human CD1b in complex with C36-GMM

Summary for 5L2J
Entry DOI10.2210/pdb5l2j/pdb
Related5L2K
DescriptorT-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 Keywordscd1b, lipid, tb, mtb, gmm, tuberculosis, gem t cell, tcr, t cell, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight48092.11
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 citationGras, 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: 27807341
DOI: 10.1038/ncomms13257
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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