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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Human beta-2 microglobulin W60V mutant structure: Implications for stability and amyloid aggregation.

Stefano Ricagno1, Sara Raimondi, Sofia Giorgetti

  • 1Department of Biomolecular Sciences and Biotechnology, CNR-INFM and CIMAINA, University of Milano, Via Celoria 26, 20133-Milano, Italy.

Biochemical and Biophysical Research Communications
|March 17, 2009
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Summary

Beta-2 microglobulin (β2m) aggregation causes dialysis-related amyloidosis. The Trp60Val mutation alters β2m stability and amyloid fibril formation, offering insights into disease mechanisms.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Medical Biochemistry

Background:

  • Beta-2 microglobulin (β2m) is the light chain of MHC-I molecules.
  • β2m is intrinsically amyloidogenic, forming cross-beta fibrils.
  • Accumulation of β2m causes dialysis-related amyloidosis, affecting joints in hemodialyzed patients.

Purpose of the Study:

  • To investigate the role of residue 60 in β2m stability and amyloid aggregation.
  • To characterize the Trp60Val (W60V) mutant's structural and aggregation properties.
  • To elucidate the function of the DE loop in β2m's propensity to form amyloid fibrils.

Main Methods:

  • Expression and purification of the W60V β2m mutant.
  • Assessment of protein folding stability (Tm) and aggregation propensity.
  • X-ray crystallography to determine the mutant's structure at 1.8Å resolution.

Main Results:

  • The W60V mutant exhibits altered folding stability and aggregation tendencies compared to wild-type β2m.
  • Structural analysis reveals specific features of the W60V mutant, particularly concerning the DE loop.
  • The study provides insights into how residue 60 influences β2m structure and amyloid formation.

Conclusions:

  • Residue 60 and the DE loop are critical determinants of β2m stability and amyloid aggregation.
  • Understanding these structural elements can inform strategies to mitigate dialysis-related amyloidosis.
  • The W60V mutant serves as a valuable model for studying β2m amyloidogenesis.