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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations

Smriti Sangwan1, Michael R Sawaya1, Kevin A Murray1

  • 1Department of Biological Chemistry Los Angeles, Howard Hughes Medical Institute, UCLA-DOE and Molecular Biology Institute, California.

Protein Science : a Publication of the Protein Society
|February 18, 2018
PubMed

Insights

Researchers uncovered the diverse structures of toxic oligomers in SOD1, a protein linked to ALS. These findings reveal key molecular features of amyloidogenic entities, advancing our understanding of protein misfolding diseases.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Amyloidogenic proteins aggregate into fibrils, forming toxic oligomeric intermediates crucial in diseases like ALS.
  • The precise structures of these oligomeric intermediates remain largely uncharacterized.

Purpose of the Study:

  • To determine the structural and biochemical characteristics of cytotoxic oligomer-forming segments of SOD1.
  • To elucidate the molecular basis of amyloid formation in SOD1.

Main Methods:

  • X-ray crystallography was used to determine the structures of variants of the SOD1 segment (residues 28-38).

Main Results:

  • Three distinct oligomeric architectures were identified: corkscrew, nontwisting curved sheet, and steric zipper proto-filament.
  • The study reveals significant polymorphism within the SOD1 segment 28-38.

Conclusions:

  • The identified structures provide insights into the molecular features of amyloidogenic entities.
  • Understanding SOD1 oligomer polymorphism is critical for deciphering its role in ALS pathogenesis.
Keywords:
ALSSOD1X-ray crystallographyamyloid fibriloligomer

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