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Major histocompatibility complex (MHC) molecules, which include human leukocyte antigens (HLAs), form an integral part of the immune response system. They are cell-surface receptors that bind foreign peptides and present them to cytotoxic T lymphocytes (CTLs). MHC class I molecules consist of two polypeptide chains, an a or heavy chain and a non-covalently associated protein, β-2-Microglobulin. The differential structural properties of MHC class I and class II molecules account for their respective roles in activating different populations of T lymphocytes. HLA-A is a MHC class I heavy chain molecule that plays a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. HLA-B and HLA-C are proteins encoded by closely related genes that also exist in the MHC class I. HLA-E belongs to the HLA class I heavy chain paralogs. HLA-E is a heterodimer consisting of a heavy chain and a light chain. The heavy chain is anchored in the membrane. HLA-E binds a restricted subset of peptides derived from the leader peptides of other class I molecules.
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