Formation of stable class II MHC/peptide complex involves conformational changes and
proceeds via an intermediate. Although this intermediate complex forms and dissociates in …

Mutational studies of T cell receptor (TCR) contact residues on the surface of the human
class I major histocompatibility complex (MHC) molecule HLA-A2 have identified a" …

The class I major histocompatibility (MHC) molecule is a heterotrimer composed of a heavy
chain, the small subunit β2-microglobulin (β2m), and a peptide. Fluorescence anisotropy …

Intracellular trafficking of major histocompatibility complex (MHC) class II molecules is
characterized by passage through specialized endocytic compartment (s) where antigenic …

A fundamental characteristic of MHC class I and class II proteins is their unusual capacity to
form stable complexes with a wide spectrum of peptide ligands. In this study, sets of peptide …

Determination of the crystal structure of class II: peptide complexes has shown that in
addition to pocket interactions involving the side chains of the peptide, peptide binding to …

Peptide binding to classical major histocompatibility complex (MHC) class II molecules is
known to be determined by the properties of the class ii peptide binding groove but recently …

The human mayor histocompatibility complex class I molecule HLA-A2 preferentially binds
peptides that contain Leu at P2 and Val or Leu at the C terminus. The other amino acids in …

Algorithms derived from measurements of short-peptide (8–10 mers) binding to class I MHC
proteins suggest that the binding groove of a class I MHC protein, such as K b, can bind well …

The ability to directly load cell surface major histocompatibility complex (MHC) class I
molecules with peptides provides a potentially powerful approach toward the development …