Class I major histocompatibility complex (MHC) molecules interact with self and foreign
peptides of diverse amino acid sequences yet exhibit distinct allele-specific selectivity for …

The ability of MHC molecules to present a broad spectrum of peptide antigens for T cell
recognition requires a compromise between high affinity and broad specificity. Three …

Considerable interest has focused on understanding how major histocompatibility complex
(MHC) specificity is generated and characterizing the specificity of MHC molecules with the …

MHC class I molecules present a variable but limited repertoire of antigenic peptides for T-
cell recognition. Understanding how peptide selection is achieved requires mechanistic …

The activation of helper T cells by peptides bound to proteins of the class II Major
Histocompatibility Complex (MHC II) is pivotal to the initiation of an immune response. The …

The peptides that bind class I MHC molecules are restricted in length and often contain key
amino acids, anchor residues, at particular positions. The side-chains of peptide anchor …

The crystal structure of a complex involving the D10 T cell receptor (TCR), 16-residue
foreign peptide antigen, and the I-Ak self major histocompatibility complex (MHC) class II …

CLASS I major histocompatibility complex (MHC) molecules present peptides to CD8+ T
cells for immunological surveillance (reviewed in ref. 1). The structures of complexes of class …

Recent developments have led to a clearer understanding of the association between
peptides and MHC molecules. It is now clear that the peptides presented by MHC class I or …

Background: Class II major histocompatibility complex (MHC) proteins are cell surface
glycoproteins that bind peptides and present them to T cells as part of the mechanism for …