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From: TSS (216-119-156-30.ipset36.wt.net)
Subject: Prion protein NMR structures of cats, dogs, pigs, and sheep
Date: January 17, 2005 at 1:07 pm PST

-------- Original Message --------
Subject: Prion protein NMR structures of cats, dogs, pigs, and sheep
Date: Sun, 16 Jan 2005 10:35:25 -0600
From: "Terry S. Singeltary Sr."
Reply-To: Bovine Spongiform Encephalopathy
To: BSE-L@LISTSERV.KALIV.UNI-KARLSRUHE.DE


##################### Bovine Spongiform Encephalopathy #####################


Prion protein NMR structures of cats, dogs, pigs, and sheep

( mammalian species | feline transmissible spongiform encephalopathy |
scrapie )

Dominikus A. Lysek, Christian Schorn *, Lucas G. Nivon {dagger} , Vicent
Esteve-Moya {ddagger} , Barbara Christen, Luigi Calzolai {sect} ,
Christine von Schroetter, Francesco Fiorito, Torsten Herrmann, Peter
Güntert ¶, and Kurt Wüthrich ||

Institut für Molekularbiologie und Biophysik, Eidgenössische Technische
Hochschule-Zürich, CH-8093 Zürich, Switzerland

Contributed by Kurt Wüthrich, December 6, 2004

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 {approx} 100 amino acid
residues and a C-terminal globular domain of {approx} 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.

------------------------------------------------------------------------

Author contributions: K.W. designed research; D.A.L., C.S., L.G.N.,
V.E.-M., B.C., L.C., C.v.S., F.F., T.H., and P.G. performed research;
and D.A.L., C.S., L.C., and K.W. wrote the paper.

*Present address: GlaxoSmithKline R&D Limited, Old Powder Mills,
Tonbridge TN11 9AN, United Kingdom.

{dagger} Present address: Department of Chemistry and Chemical Biology,
Harvard University, 12 Oxford Street, Cambridge, MA 02138.

{ddagger} Present address: Universitat de Valencia, Dr. Moliner 50,
46100-Burjassot, Valencia, Spain.

{sect} Present address: Department of Biotechnology and Molecular
Sciences, University of Insubria, Via J. Dunant 3, 21100 Varese, Italy.

¶Present address: RIKEN Genomic Sciences Center, 1-7-22 Suehiro,
Tsurumi, Yokohama 231-0045, Japan.

||To whom correspondence should be addressed.

Kurt Wüthrich, E-mail: wuthrich@mol.biol.ethz.ch


www.pnas.org/cgi/doi/10.1073/pnas.0408937102

http://www.pnas.org/cgi/content/abstract/0408937102v1

TSS


######### https://listserv.kaliv.uni-karlsruhe.de/warc/bse-l.html ##########





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