Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
Chakraborty et al. present biophysical and structural insights into fibril-forming oligomers of alpha-synuclein stabilized by heme. They show that heme targets the His50 residue of the oligomers and locks the protein into a different conformation which leads to non-toxic, non-fibrillating oligomer f...
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| Main Authors: | , , , , , , , |
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| Format: | article |
| Language: | EN |
| Published: |
Nature Portfolio
2021
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| Subjects: | |
| Online Access: | https://doaj.org/article/25742eb9b9d54e619cd7385d8ac904d4 |
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| Summary: | Chakraborty et al. present biophysical and structural insights into fibril-forming oligomers of alpha-synuclein stabilized by heme. They show that heme targets the His50 residue of the oligomers and locks the protein into a different conformation which leads to non-toxic, non-fibrillating oligomer formation, therefore addressing a very important issue in the field of structure of transient oligomers. |
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