Article
Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.
Proceedings of the National Academy of Sciences of the United States of America - 27 Oct 2009
Teilum Kaare, Smith Melanie H, Schulz Eike, Christensen Lea C, Solomentsev Gleb, Oliveberg Mikael, Akke Mikael
Abstract excerpt
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease linked to the misfolding of Cu/Zn superoxide dismutase (SOD1). ALS-related defects in SOD1 result in a gain of toxic function that coincides with aberrant oligomerization. The structural events triggering oligomerization have remained enigmatic, however, as is the case in other protein-misfolding diseases. Here, we target the critical...
Topics
- Apoenzymes
- Disulfides
- Humans
- Models, Molecular
- Mutation
- Nuclear Magnetic Resonance, Biomolecular
- Protein Multimerization
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Superoxide Dismutase
- Superoxide Dismutase-1