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Identifying the amylome, proteins capable of forming amyloid-like fibrils
Open accessAbstract
The amylome is the universe of proteins that are capable of forming amyloid-like fibrils. Here we investigate the factors that enable a protein to belong to the amylome. A major factor is the presence in the protein of a segment that can form a tightly complementary interface with an identical segment, which permits the formation of a steric zipper—two self-complementary beta sheets that form the spine of an amyloid fibril. Another factor is sufficient conformational freedom of the self-complementary segment to interact with other molecules. Using RNase A as a model system, we validate our fibrillogenic predictions by the 3D profile method based on the crystal structure of NNQQNY and demonstrate that a specific residue order is required for fiber formation. Our genome-wide analysis revealed that self-complementary segments are found in almost all proteins, yet not all proteins form amyloids. The implication is that chaperoning effects have evolved to constrain self-complementary segments from interaction with each other.
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“This is because it is considered that a majority of proteins can potentially form amyloid under suitable conditions [42,44,138,139]; insulin is another well-known human example [140–146], and the existence of a great many well-established amyloidogenic proteins above our nominal threshold of 0.7 is…”
Influential
Metadata
- Authors
- Goldschmidt, L., Teng, P. K., Riek, R., & Eisenberg, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-02-03
- Volume
- 107
- Issue
- 8
- Pages
- 3487-3492
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2129507901
- Cited by
- 809
- References
- 1
- FWCI
- 23.16
- Type
- journal article
- Language
- en
- Open access
- green
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