1xu0: Difference between revisions

Revision as of 10:03, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xu0.png

Template:STRUCTURE 1xu0

Solution structure of Xenopus leavis prion proteinSolution structure of Xenopus leavis prion protein

Template:ABSTRACT PUBMED 15647366

About this StructureAbout this Structure

1XU0 is a Single protein structure of sequence from Xenopus laevis. Full experimental information is available from OCA.

ReferenceReference

Prion protein NMR structures of chickens, turtles, and frogs., Calzolai L, Lysek DA, Perez DR, Guntert P, Wuthrich K, Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):651-5. Epub 2005 Jan 12. PMID:15647366

Page seeded by OCA on Tue Jul 29 10:03:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1xu0.gif|left|200px]]
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 {{STRUCTURE_1xu0|  PDB=1xu0  |  SCENE=  }}
-'''Solution structure of Xenopus leavis prion protein'''
+===Solution structure of Xenopus leavis prion protein===
-==Overview==
+<!--
-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 approximately 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 3(10)-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15647366}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15647366 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15647366}}
 ==About this Structure==
-XU0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XU0 OCA].
+XU0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XU0 OCA].
 ==Reference==
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 [[Category: Polymorphism]]
 [[Category: Prion]]
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