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.
|Titolo:||The three-dimensional structure of beta2 microglobulin : results from X-ray crystallography|
|Autori interni:||BOLOGNESI, MARTINO (Ultimo)|
|Parole Chiave:||β2 microglobulin; Amyloid fibril; Class I major histocompatibility complex; Cross-β structure; Dialysis related amyloidosis|
|Settore Scientifico Disciplinare:||Settore BIO/10 - Biochimica|
|Data di pubblicazione:||10-nov-2005|
|Digital Object Identifier (DOI):||10.1016/j.bbapap.2005.07.010|
|Appare nelle tipologie:||01 - Articolo su periodico|