Journal
IMMUNOLOGY
Volume 135, Issue 1, Pages 9-18Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1365-2567.2011.03515.x
Keywords
biophysics; crystal structure; peptide-major histocompatibility complex; T-cell activation; T-cell receptor
Categories
Funding
- Wales Office of Research and Development (WORD)
- BBSRC [BB/H001085/1] Funding Source: UKRI
- MRC [G0501963] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H001085/1] Funding Source: researchfish
- Medical Research Council [G0501963] Funding Source: researchfish
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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/peptidemajor 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.
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