MHC class I Recombinant Rabbit Monoclonal Antibody

Function

Major histocompatibility complex (MHC) molecules, also designated 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 β-2-Microglobulin, a non-covalently associated protein. 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. The differential structural properties of MHC class I and class II molecules account for their respective roles in activating different populations of T lymphocytes.

Background References

1. Maglietta A et al. The Immune Landscapes of Polypoid and Nonpolypoid Precancerous Colorectal Lesions. PLoS One 11:e0159373 (2016).

2. Placke T et al. Platelet-derived MHC class I confers a pseudonormal phenotype to cancer cells that subverts the antitumor reactivity of natural killer immune cells. Cancer Res 72:440-8 (2012).

Subcellular Location

Cell membrane.

UNIPROT

SwissProt: P04439 Human

Synonyms