Human beta two microglobulin: Difference between revisions
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up to 60-fold, giving rise to pathogenic accumulation of filamentous structures, displaying the | 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. | typical properties of amyloid fibrils, principally in the joints and connective tissue. | ||
__NOTOC__ | |||
==Monomeric human b2m (Mhb2m)== | ==Monomeric human b2m (Mhb2m)== | ||
The first crystal structure of Monomeric human b2m (Mhb2m) is solved in 2002 (pdb 1LDS). The protein is 99 residue in length and has a seven-stranded β sandwich fold typical of the Immunoglobulin superfamily. It is stabilized by a single disulfide bond between | The first crystal structure of Monomeric human b2m (Mhb2m) is solved in 2002 (pdb 1LDS). The protein is 99 residue in length and has a seven-stranded β sandwich fold typical of the Immunoglobulin superfamily. It is stabilized by a single disulfide bond between | ||
