Toward Molecular Dissection of PrPC-PrPSc Interactions
نویسندگان
چکیده
منابع مشابه
Immunological mimicry of PrPC-PrPSc interactions: antibody-induced PrP misfolding.
Prion diseases are associated with the conversion of cellular prion protein (PrP(C)) to an abnormal protease-resistant conformational isoform (PrP(Sc)) by template-directed conversion. The interaction between PrP(C) and PrP(Sc) is mediated by specific sites which have been mapped to six putative 'binding and conversion domains' (PrP-BCD) through peptide and antibody competition studies. Monoclo...
متن کاملMechanistic prospective for human PrPC conversion to PrPSc: Molecular dynamic insights
PrPC conversion to PrPSc isoform is the main known cause for prion diseases including Crutzfeldt-Jakob, Gerstmann-Sträussler-Sheinker syndrome and fatal familial insomnia in human. The precise mechanism underling this conversion is yet to be well understood. In the present work, using the coordinate file of PrPC (available on the Protein Data Bank) as a starting structure, separate molecular d...
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Prion diseases, also known as transmissible spongiform encephalopathies, are a group of fatal neurodegenerative diseases that include scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and Creutzfeldt-Jakob disease (CJD) in humans. The 'protein only hypothesis' advocates that PrP(Sc), an abnormal isoform of the cellular protein PrP(C), is the main and possibly sole component of ...
متن کاملPrPC was distinguished from PrPSc operationally, by the solubility in detergents and sensitivity to protease digestion of PrPC in contrast to the sedimentibility and partial resistance to proteases of PrPSc. PrPSc has a higher degree of β-sheet than PrPC
The prion hypothesis [1] is now 20 years old. In its original protein-only version, which is the one generally accepted when the term ‘prion’ or ‘prion hypothesis’ is used, protein was proposed as the sole component of the infectious agent causing the transmissible spongiform encephalopathies (TSEs), including scrapie in sheep, bovine spongiform encephalopathy (BSE) and Creutzfeldt–Jakob diseas...
متن کاملmechanistic prospective for human prpc conversion to prpsc: molecular dynamic insights
prpc conversion to prpsc isoform is the main known cause for prion diseases including crutzfeldt-jakob, gerstmann-sträussler-sheinker syndrome and fatal familial insomnia in human. the precise mechanism underling this conversion is yet to be well understood. in the present work, using the coordinate file of prpc (available on the protein data bank) as a starting structure, separate molecular d...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2007
ISSN: 0021-9258
DOI: 10.1074/jbc.m610051200