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pubmed-article:17170131pubmed:dateCreated2006-12-27lld:pubmed
pubmed-article:17170131pubmed:abstractTextThe [PSI(+)] prion of Saccharomyces cerevisiae is a self-propagating amyloid form of Sup35p, a subunit of the translation termination factor. Using solid-state NMR we have examined the structure of amyloid fibrils formed in vitro from purified recombinant Sup35(1-253), consisting of the glutamine- and asparagine-rich N-terminal 123-residue prion domain (N) and the adjacent 130-residue highly charged M domain. Measurements of magnetic dipole-dipole couplings among (13)C nuclei in a series of Sup35NM fibril samples, (13)C-labeled at backbone carbonyl sites of Tyr, Leu, or Phe residues or at side-chain methyl sites of Ala residues, indicate intermolecular (13)C-(13)C distances of approximately 0.5 nm for nearly all sites in the N domain. Certain sites in the M domain also exhibit intermolecular distances of approximately 0.5 nm. These results indicate that an in-register parallel beta-sheet structure underlies the [PSI(+)] prion phenomenon.lld:pubmed
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pubmed-article:17170131pubmed:authorpubmed-author:WicknerReed...lld:pubmed
pubmed-article:17170131pubmed:authorpubmed-author:TyckoRobertRlld:pubmed
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pubmed-article:17170131pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:17170131pubmed:year2006lld:pubmed
pubmed-article:17170131pubmed:articleTitleAmyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure.lld:pubmed
pubmed-article:17170131pubmed:affiliationLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.lld:pubmed
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