2olx

<StructureSection load='2olx' size='340' side='right' caption='[[2olx]], [[Resolution|resolution]] 1.42&Aring;' scene=''>

<table><tr><td colspan='2'>[[2olx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OLX FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yjp|1yjp]], [[1yjo|1yjo]], [[2okz|2okz]], [[2ol9|2ol9]]</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=2olx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2olx OCA], [http://pdbe.org/2olx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2olx RCSB], [http://www.ebi.ac.uk/pdbsum/2olx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2olx ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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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== References ==

[[Category: Eisenberg, D]]

[[Category: Nelson, R]]

[[Category: Sawaya, M R]]

[[Category: Asparagine zipper]]

[[Category: Steric zipper]]