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| - | [[Image:2ol9.gif|left|200px]] | |
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| - | <!--
| + | ==Peptide corresponding to residues 170-175 of human prion== |
| - | The line below this paragraph, containing "STRUCTURE_2ol9", creates the "Structure Box" on the page.
| + | <StructureSection load='2ol9' size='340' side='right'caption='[[2ol9]], [[Resolution|resolution]] 0.85Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2ol9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OL9 FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.85Å</td></tr> |
| - | --> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ol9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ol9 OCA], [https://pdbe.org/2ol9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ol9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ol9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ol9 ProSAT]</span></td></tr> |
| - | {{STRUCTURE_2ol9| PDB=2ol9 | SCENE= }}
| + | </table> |
| | | | |
| - | '''Peptide corresponding to residues 170-175 of human prion'''
| + | ==See Also== |
| - | | + | *[[Prion 3D structures|Prion 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | 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.
| + | [[Category: Homo sapiens]] |
| - | | + | [[Category: Large Structures]] |
| - | ==About this Structure==
| + | [[Category: Apostol MA]] |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OL9 OCA].
| + | [[Category: Eisenberg D]] |
| - | | + | [[Category: Sawaya MR]] |
| - | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/17468747 17468747]
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| - | [[Category: Apostol, M A.]] | + | |
| - | [[Category: Eisenberg, D.]] | + | |
| - | [[Category: Sawaya, M R]] | + | |
| - | [[Category: Beta sheet]] | + | |
| - | [[Category: Steric zipper]] | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:09:02 2008''
| + | |
