During the past year, a plethora of structural information has provided detailed insights into
the interactions between classical MHC class I molecules and their cognate receptors on T …

Neoepitopes arising from amino acid substitutions due to single nucleotide polymorphisms
are targets of T cell immune responses to cancer and are of significant interest in the …

Background Class I major histocompatibility complex (MHC) molecules bind, and present to
T cells, short peptides derived from intracellular processing of proteins. The peptide …

Loading of MHC-I molecules with peptide by the catalytic chaperone tapasin in the peptide
loading complex plays a critical role in antigen presentation and immune recognition …

T cell responsiveness to an epitope is affected both by its affinity for the presenting MHC
molecule and the affinity of the MHC-peptide complex for TCR. One limitation of cancer …

Central to CD8+ T cell–mediated immunity is the recognition of peptide–major
histocompatibility complex class I (p–MHC I) proteins displayed by antigen-presenting cells …

Immunological chaperones tapasin and TAP binding protein, related (TAPBPR) play key
roles in antigenic peptide optimization and quality control of nascent class I major …

Natural killer (NK) cell function is regulated by NK receptors that interact with MHC class I
(MHC-I) molecules on target cells. The murine NK receptor Ly49A inhibits NK cell activity by …

Chaperones TAPBPR and tapasin associate with class I major histocompatibility complexes
(MHC-I) to promote optimization (editing) of peptide cargo. Here, we use solution NMR to …

T cells recognize and respond to self antigens in both cancer and autoimmunity. One
strategy to influence this response is to incorporate amino acid substitutions into these T cell …