2on9
From Proteopedia
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+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2on9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2on9 OCA], [http://www.ebi.ac.uk/pdbsum/2on9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2on9 RCSB]</span> | ||
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[[Category: steric zipper]] | [[Category: steric zipper]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:20:16 2008'' |
Revision as of 01:20, 31 March 2008
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, resolution 1.510Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of an amyloid forming peptide VQIVYK from the repeat region of Tau
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.
About this Structure
2ON9 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Atomic structures of amyloid cross-beta spines reveal varied steric zippers., Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJ, McFarlane HT, Madsen AO, Riekel C, Eisenberg D, Nature. 2007 May 24;447(7143):453-7. Epub 2007 Apr 29. PMID:17468747
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