A structural characterization of the interaction between αβ TCRs and cognate peptide–MHC
(pMHC) is central to understanding adaptive T cell–mediated immunity. X-ray …

Although conformational changes in TCRs and peptide Ags presented by MHC protein
(pMHC) molecules often occur upon binding, their relationship to intrinsic flexibility and role …

The conformational dynamism of proteins is well established. Rather than having a single
structure, proteins are more accurately described as a conformational ensemble that exists …

T cells use the αβ TCR to bind peptides presented by MHC proteins (pMHC) on APCs.
Formation of a TCR–pMHC complex initiates T cell signaling via a poorly understood …

Dynamics plays an important but underappreciated role in the interaction between the T cell
receptor (TCR) and peptide-bound major histocompatibility complex (pMHC) …

The crystal structures of unliganded and liganded pMHC molecules provide a structural
basis for TCR recognition yet they represent 'snapshots' and offer limited insight into …

MHC-encoded molecules govern immune responses by presenting antigenic peptides to T-
cell receptors (TCRs). Several crystal structures of TCR–pMHC (peptide–MHC) complexes …

Recognition of antigenic peptides bound to major histocompatibility complex (MHC) proteins
by αβ T cell receptors (TCRs) is a hallmark of T cell mediated immunity. Recent data suggest …

CD4+ and CD8+ αβ T cell antigen recognition is determined by the interaction between the
TCR Complementarity Determining Region (CDR) loops and the peptide-presenting MHC …

Over the past two decades, structural biology has shown how T‐cell receptors engage
peptide/major histocompatibility complex (MHC) complexes and provided insight into the …