6OVN

Crystal structure of the unliganded Clone 2 TCR

Summary for 6OVN

• Entry DOI: 10.2210/pdb6ovn/pdb
• Descriptor: Alpha chain Clone 2 TCR, Beta chain Clone 2 TCR, SODIUM ION, ... (6 entities in total)
• Functional Keywords: alpha beta, t-cell receptor, receptor, immune system
• Biological source: Homo sapiens; More
• Total number of polymer chains: 2
• Total formula weight: 51545.80

Authors

Shahine, A.,Rossjohn, J. (deposition date: 2019-05-08, release date: 2019-11-20, Last modification date: 2024-11-13)

Primary citation

Reinink, P.,Shahine, A.,Gras, S.,Cheng, T.Y.,Farquhar, R.,Lopez, K.,Suliman, S.A.,Reijneveld, J.F.,Le Nours, J.,Tan, L.L.,Leon, S.R.,Jimenez, J.,Calderon, R.,Lecca, L.,Murray, M.B.,Rossjohn, J.,Moody, D.B.,Van Rhijn, I.
A TCR beta-Chain Motif Biases toward Recognition of Human CD1 Proteins.
J Immunol., 203:3395-3406, 2019

PubMed Abstract: High-throughput TCR sequencing allows interrogation of the human TCR repertoire, potentially connecting TCR sequences to antigenic targets. Unlike the highly polymorphic MHC proteins, monomorphic Ag-presenting molecules such as MR1, CD1d, and CD1b present Ags to T cells with species-wide TCR motifs. CD1b tetramer studies and a survey of the 27 published CD1b-restricted TCRs demonstrated a TCR motif in humans defined by the TCR β-chain variable gene 4-1 (TRBV4-1) region. Unexpectedly, TRBV4-1 was involved in recognition of CD1b regardless of the chemical class of the carried lipid. Crystal structures of two CD1b-specific TRBV4-1 TCRs show that germline-encoded residues in CDR1 and CDR3 regions of TRBV4-1-encoded sequences interact with each other and consolidate the surface of the TCR. Mutational studies identified a key positively charged residue in TRBV4-1 and a key negatively charged residue in CD1b that is shared with CD1c, which is also recognized by TRBV4-1 TCRs. These data show that one TCR V region can mediate a mechanism of recognition of two related monomorphic Ag-presenting molecules that does not rely on a defined lipid Ag.

PubMed: 31694911
DOI: 10.4049/jimmunol.1900872

Experimental method

X-RAY DIFFRACTION (1.77 Å)