Human beta two microglobulin

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Human Beta two microglobulin (b2m)

Beta two microglubulin in human class I major histocompatibility complex

Human β2-Microglobulin (b2m) is the non-covalently bound light chain of the human class I major histocompatibility complex (MHC-I). its function is to ensure proper folding and cell-surface expression of MHC-1. The natural turnover of MHC-I gives rise to the release of b2m into plasmatic fluids at ~0.1 um and to its catabolism in the kidney. In case of renal dysfunction, b2m concentration increases up to 60-fold, giving rise to pathogenic accumulation of filamentous structures, displaying the typical properties of amyloid fibrils, principally in the joints and connective tissue.

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Monomeric human b2m

The first crystal structure of monomeric human b2m (Mhb2m) is solved in 2002. The protein is 99 residue in length and has a seven-stranded β sandwich fold typical of the Immunoglobulin superfamily. β strands A,B,D and E comprise one β sheet, and whereas β strands C,F,G form the second β sheet. The protein is stabilized by a single disulfide bond between Cys-25 and Cys-80, which links the two β sheets.

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Jia Dong, David Canner, Michal Harel, Alexander Berchansky

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