Proteins major histocompatibility complex-associated

Homo sapiens (compared to Drosophila melanogaster) Large-scale gene duplications with substantial expansion of genes involved in acquired immune response (B cells, T cells, major histocompatibility complex genes, cytokines, chemokines and their receptors), plasma proteases (complement and hemostatic proteins), proteins associated with apoptotic regulation and proteins related to neuronal network formation and electrical coupling... 

T. H. Watts, H. E. Gaub, and H. M. McConnell, T-cell-mediated association of peptide antigen and major histocompatibility complex protein detected by energy transfer in an evanescent wave-field, Nature 320, 176-179 (1986). 

The MHC proteins are named after the "major histocompatibility complex —the DNA segment that codes for them. Human MHC proteins are also known as HLA antigens ( human leukocyte-associated antigens). Their polymorphism is so large that it is unlikely... 

Invariant chain is a transmembrane protein which temporarily associates in the ER and the Golgi apparatus with class II gene products of the major histocompatibility complex. A small portion of the invariant chain molecules carry a chondroitin sulfate chain [186]. The proteoglycan form of the invariant chain was shown to play a role in the stimulation ofT cell response [187]. 

Superantigen target three key proteins of the adaptive immune response, namely the T cell receptor (TCR), the B cell receptor (BCR) and major histocompatibility complex class II (MHC II) proteins. All are members of the Ig superfamily, and contain domains of similar tertiary structures, although MHC II contains two non-Ig-like domains. The structure of the Ig-like domain consists of two (3-sheets, each of which comprises a series of anti-parallel (3-strands, connected by loops of varying length. Ig domain structures embody two separate functions the first is the association with antigens, with each other and with other proteins, such as Fc receptors or complement, while the second is maintenance of the structural integrity of the domain itself. 

Hochstenbach, F., David, V., Watkins, S, and Brenner, M. B. (1992). Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc. Natl. Acad. Sci USA 89, 4734-4738. 

Balow, J. P., Weissman, J. D., and Kearse, K. P. (1995). Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association./. Biol. Chem. 270, 29025-29029. 

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