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Stable major histocompatibility complex (MHC) class I molecules at the cell surface consist of three separate, noncovalently associated components: the class I heavy chain, the 2-microglobulin light chain, and a presented peptide.
MHC I consists of heavy (H) and light (L) chains, with the L chain being an invariant protein partner called -2 microglobulin (2m), respectively (Fig 1). Following assembly within the Endoplasmic Reticulum (ER), the HLA is unstable in the absence of a peptide ligand [20,21].
H-2M plays a vital role in the removal of CLIP and for allowing peptide epitopes to bind to the class II MHC molecules. In the absence of H-2M, CLIP would prevent the binding of antigens in the binding groove and their subsequent presentation on the cell surface (7).
Class I MHC proteins consist of a transmembrane chain, which is encoded by a class I MHC gene, and a small extracellular protein called 2-microglobulin (Figure 24-49A). The 2-microglobulin does not span the membrane and is encoded by a gene that does not lie in the MHC gene cluster.
Cutting edge: single-chain trimers of MHC class I molecules form stable structures that potently stimulate antigen-specific T cells and B cells. SCT is a polypeptide in which the three components, a peptide, 2m and the MHC class I heavy chain are joined together via flexible linkers.

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Abstract. Class I major histocompatibility complex (MHC) molecules are ternary complexes of the soluble serum protein beta 2-microglobulin, MHC heavy chain, and bound peptide. The first two domains (alpha 1, alpha 2) of the heavy chain create the peptide binding cleft and the surface that contacts the T-cell receptor.

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