Residues within processed protein fragments bound to major histocompatibility complex
class I (MHC-I) glycoproteins have been considered to function as a series of “independent …

Peptide loading of major histocompatibility complex (MHC) class II molecules in the
endosomes and lysosomes of antigen-presenting cells is catalyzed by human leukocyte …

Small peptides, derived from endogenous proteins bind within the antigen binding groove
created by the beta-pleated sheets and alpha helices of the alpha 1 and alpha 2 domains of …

It is well established that even small changes in amino acid side chains of antigenic peptide
bound to major histocompatibility complex (MHC) protein may completely abrogate …

We have previously identified four anchor positions in HLA-DRB1* 0101-binding peptides,
and three anchors involved in peptide binding to DRB1* 0401 and DRB1* 1101 molecules …

MHC class I and MHC class II molecules present peptides to the immune system to drive
proper T cell responses. Pharmacological modulation of T-cell responses can offer treatment …

Unusually long major histocompatibility complex (MHC) class I–restricted epitopes are
important in immunity, but their'bulged'conformation represents a potential obstacle to αβ T …

CD8+ T cells express T cell receptors (TCRs) that recognize short peptide antigens in the
context of major histocompatibility class I (MHC I) molecules. This recognition process …

Class I major histocompatibility complex (MHC) molecules, which display intracellularly
processed peptides on the cell surface for scanning by T-cell receptors (TCRs), are …

The immune system has developed a variety of mecharmisms for sensing the presence of
invading microorganisms, which must be accomplished in the face of special topological …