The three-dimensional structure of β2 microglobulin: Results from X-ray crystallography

Camillo Rosano, Simone Zuccotti, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review

Abstract

β2-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 β2-microglobulin component, dissociated form the complex heavy chain, gives rise to amyloidogenic deposits in the joints of patients exposed to long dialysis periods. β2-microglobulin three-dimensional structure is based on an antiparallel β-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 β2-microglobulin can be related to local unfolding, to the tendency to aggregate laterally through non-compensated β-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 β2-microglobulin as an isolated chain, separated form the major histocompatibility complex I heavy chain.

Original languageEnglish
Pages (from-to)85-91
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1753
Issue number1
DOIs
Publication statusPublished - Nov 10 2005

Keywords

  • β2 microglobulin
  • Amyloid fibril
  • Class I major histocompatibility complex
  • Cross-β structure
  • Dialysis related amyloidosis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics

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