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5D7K

Structure of MR1-reactive MAV36 TCR

Summary for 5D7K
Entry DOI10.2210/pdb5d7k/pdb
Related5D5M 5D7I 5D7J 5D7L
DescriptorMAV36 TCR Alpha Chain, MAV36 TCR Beta Chain, SULFATE ION, ... (4 entities in total)
Functional Keywordsreceptor, antigen, immune system
Biological sourceHomo sapiens
More
Total number of polymer chains2
Total formula weight50850.95
Authors
Keller, A.N.,Rossjohn, J. (deposition date: 2015-08-14, release date: 2016-01-27, Last modification date: 2024-10-16)
Primary citationGherardin, N.A.,Keller, A.N.,Woolley, R.E.,Le Nours, J.,Ritchie, D.S.,Neeson, P.J.,Birkinshaw, R.W.,Eckle, S.B.,Waddington, J.N.,Liu, L.,Fairlie, D.P.,Uldrich, A.P.,Pellicci, D.G.,McCluskey, J.,Godfrey, D.I.,Rossjohn, J.
Diversity of T Cells Restricted by the MHC Class I-Related Molecule MR1 Facilitates Differential Antigen Recognition.
Immunity, 44:32-45, 2016
Cited by
PubMed Abstract: A characteristic of mucosal-associated invariant T (MAIT) cells is the expression of TRAV1-2(+) T cell receptors (TCRs) that are activated by riboflavin metabolite-based antigens (Ag) presented by the MHC-I related molecule, MR1. Whether the MR1-restricted T cell repertoire and associated Ag responsiveness extends beyond these cells remains unclear. Here, we describe MR1 autoreactivity and folate-derivative reactivity in a discrete subset of TRAV1-2(+) MAIT cells. This recognition was attributable to CDR3β loop-mediated effects within a consensus TRAV1-2(+) TCR-MR1-Ag footprint. Furthermore, we have demonstrated differential folate- and riboflavin-derivative reactivity by a diverse population of "atypical" TRAV1-2(-) MR1-restricted T cells. We have shown that TRAV1-2(-) T cells are phenotypically heterogeneous and largely distinct from TRAV1-2(+) MAIT cells. A TRAV1-2(-) TCR docks more centrally on MR1, thereby adopting a markedly different molecular footprint to the TRAV1-2(+) TCR. Accordingly, diversity within the MR1-restricted T cell repertoire leads to differing MR1-restricted Ag specificity.
PubMed: 26795251
DOI: 10.1016/j.immuni.2015.12.005
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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