Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin
Integrated kinetic and structural investigations reveal that the ubiquitous co-chaperonin prefoldin interacts with its coiled-coil helices on the islet amyloid polypeptide fibril surface and fibril ends to inhibit fibril elongation and secondary nucleation.
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-30042-y |