The three-dimensional structure of beta2 microglobulin: results from X-ray crystallography.
beta2-microglobulin, the light chain component of the major histocompatibility complex I, is involved in the development of DRA, an amyloid deposition disease occurring in man. Specifically, the beta2-microglobulin component, dissociated form the complex heavy chain, gives rise to amyloidogenic deposits in the joints of patients exposed to long dialysis periods. beta2-microglobulin three-dimensional structure is based on an antiparallel beta-barrel fold, with immunoglobulin domain topology, displaying structural flexibility in the crystal and NMR structures so fare determined. The structural bases of amyloidogenic potential in beta2-microglobulin can be related to local unfolding, to the tendency to aggregate laterally through non-compensated beta-strands, and partly also to its trend towards N-terminal proteolytic degradation. Such trends emerge quite clearly from inspection of a limited number of crystal structures of beta2-microglobulin as an isolated chain, separated form the major histocompatibility complex I heavy chain.
Rosano
Camillo
C
Bioinformatics and Structural Proteomics, National Institute for Cancer Research (IST), Largo R. Benzi 10, 16132 Genova, Italy. camillo.rosano@istge.it
Zuccotti
Simone
S
Bolognesi
Martino
M
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D000686:Amyloidosis / Q000209:etiology; D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D006801:Humans; D017433:Protein Structure, Secondary; D006435:Renal Dialysis / Q000009:adverse effects; D016415:Sequence Alignment; D001613:beta 2-Microglobulin / Q000737:chemistry* / Q000235:genetics
D000682:Amyloid; D001613:beta 2-Microglobulin