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The Three-Dimensional Structures of Amyloids.

Roland Riek1

  • 1Laboratory of Physical Chemistry, ETH Zürich, 8093 Zürich, Switzerland.

Cold Spring Harbor Perspectives in Biology
|October 30, 2016
PubMed
Summary
This summary is machine-generated.

Amyloids are protein aggregates with a unique cross-β-sheet structure. This structure enables diverse biological functions and disease associations, including prion diseases and neurodegeneration.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Amyloids are ordered protein aggregates linked to diseases like Alzheimer's and Parkinson's, as well as biological functions.
  • Their defining feature is the cross-β-sheet motif, a repeating two-layered intermolecular structure.
  • This unique fold forms through intermolecular contacts, requiring only short amino acid sequences.

Purpose of the Study:

  • To review the structural nature of the cross-β-sheet motif in amyloids.
  • To explore the relationship between amyloid structure and biological activities.
  • To summarize findings from high-resolution structural studies.

Main Methods:

  • Review of high-resolution structural studies of amyloids.
  • Analysis of the cross-β-sheet structural motif.
  • Correlation of structural properties with observed biological activities.

Main Results:

  • Amyloid structure is characterized by a repeating cross-β-sheet entity (repeating every 4.7 Å).
  • The structure facilitates growth by recruiting peptides, enabling infectivity (prions).
  • Repetitiveness enhances monomeric activity through cooperativity, leading to diverse functions.

Conclusions:

  • Amyloid cross-β-sheet structure is fundamental to their diverse activities, including infectivity and gain/loss of function.
  • Structural insights explain amyloid properties like potentiation of activity and toxicity.
  • Understanding amyloid structure is key to elucidating their roles in disease and biology.