SEARCH VEGSOURCE:

 

 

Follow Ups | Post Followup | Back to Discussion Board | VegSource
See spam or
inappropriate posts?
Please let us know.
  




From: TSS (216-119-156-30.ipset36.wt.net)
Subject: Prion protein NMR structures of chickens, turtles, and frogs
Date: January 17, 2005 at 1:05 pm PST

-------- Original Message --------
Subject: Prion protein NMR structures of chickens, turtles, and frogs
Date: Sun, 16 Jan 2005 10:35:40 -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 chickens, turtles, and frogs

( nonmammalian species | transmissible spongiform encephalopathy )

Luigi Calzolai *{dagger} {ddagger} , Dominikus A. Lysek *{dagger} ,
Daniel R. Pérez *{dagger} {sect} , Peter Güntert *¶, and Kurt Wüthrich *||

*Institut für Molekularbiologie und Biophysik, Eidgenössische Technische
Hochschule Zürich, CH-8093 Zürich, Switzerland; and {sect} Graduate
Program in Molecular, Cellular, and Neuroscience Biology, Facultad de
Ciencias, Universidad de Chile, Casilla 653, Santiago, Chile

Contributed by Kurt Wüthrich, December 6, 2004

The NMR structures of the recombinant prion proteins from chicken
(Gallus gallus; chPrP), the red-eared slider turtle (Trachemys scripta;
tPrP), and the African clawed frog (Xenopus laevis; xlPrP) are
presented. The amino acid sequences of these prion proteins show
{approx} 30% identity with mammalian prion proteins. All three species
form the same molecular architecture as mammalian PrPC, with a long,
flexibly disordered tail attached to the N-terminal end of a globular
domain. The globular domain in chPrP and tPrP contains three {alpha}
-helices, one short 310-helix, and a short antiparallel {beta} -sheet.
In xlPrP, the globular domain includes three {alpha} -helices and a
somewhat longer {beta} -sheet than in the other species. The spatial
arrangement of these regular secondary structures coincides closely with
that of the globular domain in mammalian prion proteins. Based on the
low sequence identity to mammalian PrPs, comparison of chPrP, tPrP, and
xlPrP with mammalian PrPC structures is used to identify a set of
essential amino acid positions for the preservation of the same PrPC
fold in birds, reptiles, amphibians, and mammals. There are additional
conserved residues without apparent structural roles, which are of
interest for the ongoing search for physiological functions of PrPC in
healthy organisms.

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

Author contributions: K.W. designed research; L.C., D.A.L., D.R.P., and
P.G. performed research; and L.C., D.A.L., D.R.P., and K.W. wrote the paper.

{dagger} L.C., D.A.L., and D.R.P. contributed equally to this work.

{ddagger} 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.0408939102

http://www.pnas.org/cgi/content/abstract/0408939102v1

TSS


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





Follow Ups:



Post a Followup

Name:
E-mail: (optional)
Subject:

Comments:

Optional Link URL:
Link Title:
Optional Image URL: