Major histocompatibility complex (MHC), human leukocyte antigen (HLA) molecules are cell-surface receptors that bind foreign peptides and present them to T lymphocytes. MHC class I molecules consist of two polypeptide chains, an a or heavy chain, and a non-covalently associated protein, b-2-microglobulin. Cytotoxic T lymphocytes bind antigenic peptides presented by MHC class I molecules. Antigens that bind to MHC class I molecules are typically 8-10 residues in length and are stabilized in a peptide binding groove. MHC class II molecules are encoded by polymorphic MHC genes and consist of a non-covalent complex of an a and b chain. Helper T lymphocytes bind antigenic peptides presented by MHC class II molecules. MHC class II molecules bind 13-18 amino acid antigenic peptides. Accumulating in endosomal/lysosomal compartments and on the surface of B cells, HLA-DM and -DO molecules regulate binding of exogenous peptides to class II molecules (HLA-DR) by sustaining a conformation that favors peptide exchange.