ArticleBiomolecular NMR assignments2016
Backbone resonance assignment of N15, N30 and D10 T cell receptor β subunits.
Article in Biomolecular NMR assignments, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Efficient and economic protein labeling for NMR in mammalian expression systems: Application to a preT-cell and T-cell receptor protein.Protein science : a publication of the Protein Society · 2024Article
- NMR: an essential structural tool for integrative studies of T cell development, pMHC ligand recognition and TCR mechanobiology.Journal of biomolecular NMR · 2019Article
- NMR-directed design of pre-TCRβ and pMHC molecules implies a distinct geometry for pre-TCR relative to αβTCR recognition of pMHC.The Journal of biological chemistry · 2018Article
- A general chemical crosslinking strategy for structural analyses of weakly interacting proteins applied to preTCR-pMHC complexes.The Journal of biological chemistryArticle
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Authors and funding
4 authors.
Funding
Abstract
The αβT Cell receptor (TCR) governs T cell immunity through its interaction with peptide bound to major histocompatibility complex molecules (pMHC). Previously, soluble ectodomain constructs have been used to elucidate the binding mode of the TCR for the MHC. However, the full heterodimeric αβTCR has proven difficult to produce reproducibly in recombinant systems to the extent seen in the routine production of novel antibodies. Particularly, the route of production in E. coli, which is most convenient for isotopic labeling of proteins, is challenging for a wide range of αβTCR, including N15αβ, N30αβ, but not D10αβ. With the aim of understanding the TCR-pMHC interaction through the use of dynamic binding measurements, we set out to produce TCRβ subunits with which we could investigate binding with pMHC. The TCRβ constructs are more readily produced and refolded than their αβ counterparts and have proven to be an effective model of preTCR in pMHC binding studies. As a first step towards characterizing potential interactions with protein ligands, we have assigned the backbone resonances of three TCRβ subunits, N15β, N30β and D10β.
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