2onv

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[[Image:2onv.png|left|200px]]
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==Crystal Structure of the amyloid-fibril forming peptide GGVVIA derived from the Alzheimer's amyloid Abeta (Abeta37-42).==
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<StructureSection load='2onv' size='340' side='right' caption='[[2onv]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2onv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ONV FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2onv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2onv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2onv RCSB], [http://www.ebi.ac.uk/pdbsum/2onv PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2onv| PDB=2onv | SCENE= }}
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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<ref>PMID:17468747</ref>
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===Crystal Structure of the amyloid-fibril forming peptide GGVVIA derived from the Alzheimer's amyloid Abeta (Abeta37-42).===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_17468747}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2onv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONV OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:017468747</ref><references group="xtra"/>
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[[Category: Eisenberg, D.]]
[[Category: Eisenberg, D.]]
[[Category: Sambashivan, S.]]
[[Category: Sambashivan, S.]]

Revision as of 11:22, 20 October 2014

Crystal Structure of the amyloid-fibril forming peptide GGVVIA derived from the Alzheimer's amyloid Abeta (Abeta37-42).

2onv, resolution 1.61Å

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