Abstract
T cells are a critical part of the adaptive immune system that are able to distinguish between healthy and unhealthy cells. Upon recognition of protein fragments (peptides), activated T cells will contribute to the immune response and help clear infection. The major histocompatibility complex (MHC) molecules, or human leukocyte antigens (HLA) in humans, bind these peptides to present them to T cells that recognise them with their surface T cell receptors (TCR). This recognition event is the first step that leads to T cell activation, and in turn can dictate disease outcomes. The visualisation of TCR interaction with pMHC using structural biology has been crucial in understanding this key event, unravelling the parameters that drive this interaction and their impact on the immune response. The last five years has been the most productive within the field, wherein half of current unique TCR–pMHC-I structures to date were determined within this time. Here, we review the new insights learned from these recent TCR–pMHC-I structures and their impact on T cell activation.
Highlights
T cells are a critical part of the adaptive immune system that are able to distinguish between healthy and unhealthy cells
We focus on the T cell receptors (TCR) recognition of peptide (p) presented by major histocompatibility complex (MHC) class I (MHC-I) molecules only
This conserved localisation of the TCR ensures that the peptide and the MHC-I helices are always contacted by the TCR
Summary
T cells use their surface receptor, called T cell receptor or TCR, to recognise peptides presented by major histocompatibility complex (MHC) molecules. [12]; HLA-A*02:06 the most [13]; and, for the firstSome time, of HLA-C [14].striking features revealed over the last few years include the first reversed docking MHC-I restricted TCR [15], how a TCR can flip the peptide upon binding [16], how δβ and γδ TCRs recognise pMHC [17,18,19], and the revelation of new rules defining TCR cross-reactivity [20]. Some of the most striking features revealed over the last few years include the first reversed docking MHC-I restricted TCR [15], how a TCR can flip the peptide upon binding [16], how δβ and γδ TCRs recognise pMHC [17,18,19], and the revelation of new rules defining TCR cross-reactivity [20]
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