1xu0: Difference between revisions

New page: left|200px<br /><applet load="1xu0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xu0" /> '''Solution structure of Xenopus leavis prion p...
 
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'''Solution structure of Xenopus leavis prion protein'''<br />


==Overview==
==Solution structure of Xenopus leavis prion protein==
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.
<StructureSection load='1xu0' size='340' side='right'caption='[[1xu0]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xu0]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XU0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu0 OCA], [https://pdbe.org/1xu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1xu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xu0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5S1W7_XENLA Q5S1W7_XENLA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xu/1xu0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xu0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==About this Structure==
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<ref>PMID:15647366</ref>
1XU0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XU0 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15647366 15647366]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1xu0" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Prion 3D structures|Prion 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Perez, D.R.]]
[[Category: Perez DR]]
[[Category: Wuthrich, K.]]
[[Category: Wuthrich K]]
[[Category: amphibian]]
[[Category: glycoprotein]]
[[Category: polymorphism]]
[[Category: prion]]
 
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