1y2s
From Proteopedia
|
Ovine Prion Protein Variant R168
Overview
The NMR structures of the recombinant cellular form of the prion proteins, (PrPC) of the cat (Felis catus), dog (Canis familiaris), and pig (Sus, scrofa), and of two polymorphic forms of the prion protein from sheep, (Ovis aries) are presented. In all of these species, PrPC consists of an, N-terminal flexibly extended tail with approximately 100 amino acid, residues and a C-terminal globular domain of approximately 100 residues, with three alpha-helices and a short antiparallel beta-sheet. Although, this global architecture coincides with the previously reported murine, Syrian hamster, bovine, and human PrPC structures, there are local, differences between the globular domains of the different species. Because, the five newly determined PrPC structures originate from species with, widely different transmissible spongiform encephalopathy records, the, present data indicate previously uncharacterized possible correlations, between local features in PrPC three-dimensional structures and, susceptibility of different mammalian species to transmissible spongiform, encephalopathies.
About this Structure
1Y2S is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.
Reference
Prion protein NMR structures of cats, dogs, pigs, and sheep., Lysek DA, Schorn C, Nivon LG, Esteve-Moya V, Christen B, Calzolai L, von Schroetter C, Fiorito F, Herrmann T, Guntert P, Wuthrich K, Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):640-5. Epub 2005 Jan 12. PMID:15647367
Page seeded by OCA on Wed Nov 21 06:31:24 2007
Categories: Ovis aries | Single protein | Christen, B. | Herrmann, T. | Lysek, D.A. | Wuthrich, K. | Glycoprotein | Gpi-anchor | Ovprp | Polymorphism | Prion protein | Scrapie | Sheep | Tse
