Human beta two microglobulin: Difference between revisions
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Human β2-Microglobulin (b2m) is the non-covalently bound light chain of the human class I | Human β2-Microglobulin (b2m) is the non-covalently bound light chain of the human class I | ||
major histocompatibility complex (MHC-I). | major histocompatibility complex (MHC-I). | ||
its function is to ensure proper folding and cell-surface expression of MHC-1. | 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 | The natural turnover of MHC-I gives rise to the release of b2m into plasmatic fluids at ~0.1 | ||
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The first crystal structure of monomeric human b2m (Mhb2m) is solved in 2002. The protein is 99 residue in length and has a | 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 | 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, | whereas β strands C,F,G form the second β sheet. The protein is stabilized by a single disulfide bond between Cys-25 and | ||
which links the two β sheets. | Cys-80,which links the two β sheets. | ||
{{STRUCTURE_1lds | PDB=1lds | SCENE= }} | |||
Structural comparison of human b2m bound to MHC-1 (left) and monomeric human b2m (right) | |||
[[Image:Human b2m bound to MHC-1 .jpg.jpg]] [[Image:Momeric human b2m.png]] | |||
The | |||
