1yjo
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(New page: 200px<br /><applet load="1yjo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yjo, resolution 1.30Å" /> '''Structure of NNQQNY ...)
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Revision as of 04:43, 21 November 2007
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Structure of NNQQNY from yeast prion Sup35 with zinc acetate
Overview
Numerous soluble proteins convert to insoluble amyloid-like fibrils that, have common properties. Amyloid fibrils are associated with fatal diseases, such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For, the yeast protein Sup35, conversion to amyloid-like fibrils is associated, with a transmissible infection akin to that caused by mammalian prions. A, seven-residue peptide segment from Sup35 forms amyloid-like fibrils and, closely related microcrystals, from which we have determined the atomic, structure of the cross-beta spine. It is a double beta-sheet, with each, sheet formed from parallel segments stacked in register. Side chains, protruding from the two sheets form a dry, tightly self-complementing, steric zipper, bonding the sheets. Within each sheet, every segment is, bound to its two neighbouring segments through stacks of both backbone and, side-chain hydrogen bonds. The structure illuminates the stability of, amyloid fibrils, their self-seeding characteristic and their tendency to, form polymorphic structures.
About this Structure
1YJO is a Single protein structure of sequence from [1] with ZN and ACY as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the cross-beta spine of amyloid-like fibrils., Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D, Nature. 2005 Jun 9;435(7043):773-8. PMID:15944695
Page seeded by OCA on Wed Nov 21 06:50:41 2007
