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The protofilament structure of insulin amyloid fibrils
Open accessAbstract
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-β structure. However, there is a lack of information relating the 4.8 Å β-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 protofilament packing indicate that the cross-β ribbon is composed of relatively flat β-sheets rather than being the highly twisted, β-coil structure previously suggested by analysis of globular protein folds. Comparison of the various fibril structures suggests that very small, local changes in β-sheet twist are important in establishing the long-range coiling of the protofilaments into fibrils of diverse morphology.
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Metadata
- Authors
- Jiménez, J. L., Nettleton, E. J., Bouchard, M., Robinson, C. V., Dobson, C. M., & Saibil, H. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-07
- Volume
- 99
- Issue
- 14
- Pages
- 9196-9201
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2101614182
- Cited by
- 834
- References
- 0
- FWCI
- 16.90
- Type
- journal article
- Language
- en
- Open access
- green
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