5L2K

Crystal structure of GEM42 TCR-CD1b-GMM complex

Summary for 5L2K

• Entry DOI: 10.2210/pdb5l2k/pdb
• Related: 5L2J
• Descriptor: T-cell surface glycoprotein CD1b, CESIUM ION, 6-O-[(2R,3R)-3-hydroxy-2-tetradecyldocosanoyl]-alpha-L-idopyranose, ... (12 entities in total)
• Functional Keywords: cd1b, lipid, tb, mtb, gmm, tuberculosis, gem t cell, tcr, t cell, gem42, immune system
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 97837.01

Authors

Gras, S.,Shahine, A.,Le Nours, J.,Rossjohn, J. (deposition date: 2016-08-02, release date: 2016-11-16, Last modification date: 2024-10-09)

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

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)