2omm: Difference between revisions

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==Overview==

Amyloid fibrils formed from different proteins, each associated with a, particular disease, contain a common cross-beta 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 beta-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-beta and tau proteins, the PrP prion, protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, alpha-synuclein and beta(2)-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.

Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-beta 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 beta-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-beta and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, alpha-synuclein and beta(2)-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.

==About this Structure==

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[[Category: Eisenberg, D.]]

[[Category: Nelson, R.]]

[[Category: Sawaya, M.R.]]

[[Category: Sawaya, M R.]]

[[Category: asparagine zipper]]

[[Category: glutamine zipper]]

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[[Category: steric zipper]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Amyloid fibrils formed from different proteins, each associated with a, particular disease, contain a common cross-beta 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 beta-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-beta and tau proteins, the PrP prion, protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, alpha-synuclein and beta(2)-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.
+Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-beta 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 beta-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-beta and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, alpha-synuclein and beta(2)-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.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Eisenberg, D.]]
 [[Category: Nelson, R.]]
-[[Category: Sawaya, M.R.]]
+[[Category: Sawaya, M R.]]
 [[Category: asparagine zipper]]
 [[Category: glutamine zipper]]
@@ Line 20: / Line 20: @@
 [[Category: steric zipper]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:58:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:11 2008''