Abstract | ||
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T cells play a critical role in the adaptive immune response. They perform their function by recognizing infected cells presenting peptides on a specialized complex known as the MHC. The recognition process involves binding of the peptide-loaded MHC to the T cell receptor (TCR), a surface molecule comprised of an alpha and a beta chain. A large body of evidence suggests that T cells can respond to previously unseen pathogens, a phenomenon known as cross-reactivity. Cross-reactivity has important medical implications, as cross-reactive responses can be either protective or lead to disease. A possible mechanism that has been proposed to explain cross-reactivity is the differential usage of the alpha and beta chains, whereas one peptide can be recognized predominantly by the alpha chain and a different peptide by the beta chain. In this study we carry out a systematic analysis of a non-redundant set of 67 crystal structures, measuring TCR alpha/beta usage and its relationship with structural features of the interaction. Our results show a wide range of TCR alpha/beta usage in different complexes. Further, we find that alpha/beta usage significantly correlates with one of the docking angles between the TCR and the MHC. |
Year | DOI | Venue |
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2017 | 10.1109/BIBM.2017.8217629 | 2017 IEEE International Conference on Bioinformatics and Biomedicine (BIBM) |
Keywords | DocType | ISSN |
beta chain,T cells,alpha chain,crystal structures,TCR alpha-beta usage,T cell receptor alpha-beta usage,pMHC,peptide-loaded MHC,disease | Conference | 2156-1125 |
ISBN | Citations | PageRank |
978-1-5090-3051-4 | 0 | 0.34 |
References | Authors | |
0 | 2 |
Name | Order | Citations | PageRank |
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Ryan Ehrlich | 1 | 0 | 0.34 |
Dario Ghersi | 2 | 66 | 7.04 |