Atomic structures of amyloid cross-β spines reveal varied steric zippers

Michael R. Sawaya; Shilpa Sambashivan; Rebecca Nelson; Magdalena I. Ivanova; Stuart A. Sievers; Marcin I. Apostol; Michael J. Thompson; Melinda Balbirnie; Jed J.W. Wiltzius; Heather T. McFarlane; Anders Madsen; Christian Riekel; David Eisenberg

doi:10.1038/nature05695

Atomic structures of amyloid cross-β spines reveal varied steric zippers

Michael R. Sawaya, Shilpa Sambashivan, Rebecca Nelson, Magdalena I. Ivanova, Stuart A. Sievers, Marcin I. Apostol, Michael J. Thompson, Melinda Balbirnie, Jed J.W. Wiltzius, Heather T. McFarlane, Anders Madsen, Christian Riekel, David Eisenberg^*

^*Corresponding author for this work

1637 Citations (Scopus)

Abstract

Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of β-sheets, with the facing side chains of the two sheets interdigitated in a dry 'steric zipper'. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer's amyloid-β and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, α-synuclein and β₂-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.

Original language	English
Journal	Nature
Volume	447
Issue number	7143
Pages (from-to)	453-457
Number of pages	5
ISSN	0028-0836
DOIs	https://doi.org/10.1038/nature05695
Publication status	Published - 24 May 2007

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title = "Atomic structures of amyloid cross-β spines reveal varied steric zippers",

abstract = "Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of β-sheets, with the facing side chains of the two sheets interdigitated in a dry 'steric zipper'. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer's amyloid-β and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, α-synuclein and β2-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.",

author = "Sawaya, {Michael R.} and Shilpa Sambashivan and Rebecca Nelson and Ivanova, {Magdalena I.} and Sievers, {Stuart A.} and Apostol, {Marcin I.} and Thompson, {Michael J.} and Melinda Balbirnie and Wiltzius, {Jed J.W.} and McFarlane, {Heather T.} and Anders Madsen and Christian Riekel and David Eisenberg",

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T1 - Atomic structures of amyloid cross-β spines reveal varied steric zippers

AU - Sawaya, Michael R.

AU - Sambashivan, Shilpa

AU - Nelson, Rebecca

AU - Ivanova, Magdalena I.

AU - Sievers, Stuart A.

AU - Apostol, Marcin I.

AU - Thompson, Michael J.

AU - Balbirnie, Melinda

AU - Wiltzius, Jed J.W.

AU - McFarlane, Heather T.

AU - Madsen, Anders

AU - Riekel, Christian

AU - Eisenberg, David

PY - 2007/5/24

Y1 - 2007/5/24

N2 - Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of β-sheets, with the facing side chains of the two sheets interdigitated in a dry 'steric zipper'. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer's amyloid-β and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, α-synuclein and β2-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.

AB - Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of β-sheets, with the facing side chains of the two sheets interdigitated in a dry 'steric zipper'. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer's amyloid-β and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, α-synuclein and β2-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.

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Atomic structures of amyloid cross-β spines reveal varied steric zippers

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