The protofilament structure of insulin amyloid fibrils
University of Oxford · Birkbeck, University of London
Abstract
Under solution conditions where the native state is destabilized, the largely helical polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic cross-beta structure. However, there is a lack of information relating the 4.8 A beta-strand repeat to the higher order assembly of amyloid fibrils. We have used cryo-electron microscopy (EM), combining single particle analysis and helical reconstruction, to characterize these fibrils and to study the three-dimensional (3D) arrangement of their component protofilaments. Low-resolution 3D structures of fibrils containing 2, 4, and 6 protofilaments reveal a characteristic, compact shape of the insulin protofilament. Considerations of…
Citation impact
- FWCI
- 14.46
- Percentile
- 100%
- References
- 41
Authors
6- JLJosé L. JiménezCorresponding
University of Oxford, Birkbeck, University of London
- EJEwan J. Nettleton
University of Oxford, Birkbeck, University of London
- MBMario Bouchard
University of Oxford, Birkbeck, University of London
- CVCarol V. Robinson
University of Oxford, Birkbeck, University of London
- CMChristopher M. Dobson
University of Oxford, Birkbeck, University of London
Topics & keywords
- Fibril
- Crystallography
- Biophysics
- Amyloid (mycology)
- Globular protein
- Cryo-electron microscopy
- Amyloid fibril
- Protein structure