Bridgeman, John S., Sewell, Andrew K.  ORCID: https://orcid.org/0000-0003-3194-3135, Miles, John James, Price, David A. ORCID: https://orcid.org/0000-0001-9416-2737 and Cole, David K. ORCID: https://orcid.org/0000-0003-0028-9396
2012.
Structural and biophysical determinants of ab T-cell antigen
recognition.
Immunology
135
(1)
, pp. 9-18.
10.1111/j.1365-2567.2011.03515.x
|
Abstract
The molecular rules that govern MHC restriction, and allow T-cells to differentiate between peptides derived from healthy cells and those from diseased cells, remain poorly understood. Here we provide an overview of the structural constraints that enable the T-cell receptor (TCR) to discriminate between self and non-self peptides, and summarize studies that have attempted to correlate the biophysical parameters of TCR/peptide–major histocompatibility complex (pMHC) binding with T-cell activation. We further review how the antigenic origin of peptide epitopes affects TCR binding parameters and the ‘quality’ of a T-cell response. Understanding the principles that govern pMHC recognition by T-cells will unlock pathways to the rational development of immunotherapeutic approaches for the treatment of infectious disease, cancer and autoimmunity.
| Item Type: | Article |
|---|---|
| Date Type: | Publication |
| Status: | Published |
| Schools: | Schools > Medicine Research Institutes & Centres > Systems Immunity Research Institute (SIURI) |
| Subjects: | R Medicine > R Medicine (General) |
| Uncontrolled Keywords: | biophysics; crystal structure; peptide-major histocompatibility complex; T-cell activation; T-cell receptor |
| Publisher: | Wiley Blackwell |
| ISSN: | 0019-2805 |
| Last Modified: | 10 Jun 2023 01:08 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/26503 |
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