## Abstract __αβ__ T‐cell receptors (TCRs) recognize peptide antigens presented by class I or class II major histocompatibility complex molecules (pMHC). Here we review the use of thermodynamic measurements in the study of TCR–pMHC interactions, with attention to the diversity in binding thermodyna
T-cell receptor peptide-MHC interactions: biological lessons from structural studies
✍ Scribed by K Christopher Garcia; Luc Teyton
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 385 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0958-1669
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✦ Synopsis
Fifteen years have passed since T-cell receptor (TCR) genes were identified (reviewed in [1]). Unlike the situation for antibodies, no direct structural information on the TCR proteins has been available for most of this time. Recently, however, the crystal structures of isolated (z and ~ chains were determined, shortly followed by the determination of the structure of an cq3 heterodimer. Subsequently, the structures of two TCR peptide-MHC (pMHC) complexes have been reported. The windfall of this, and other more recent structural information, has elucidated some generalizations for TCR binding and recognition of pMHC. The crystal structures have, however, given us very little insight into the mechanisms of signal transduction by the TCR complex and the subsequent events which lead to activation of a T cell. Ultimately, the crystallographic results will be reconciled with experiments from other disciplines for a complete understanding of the molecular events of T cell activation
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## Abstract The advent in recent years of the application of tetrameric arrays of class I peptide–MHC complexes now enables us to detect and study rare populations of antigen‐specific CD8+ T cells. However, available methods cannot visualize or determine the number and distribution of these TCR lig