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New page: left|200px<br /><applet load="1i17" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i17" /> '''NMR STRUCTURE OF MOUSE DOPPEL 51-157'''<br /...
 
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[[Image:1i17.gif|left|200px]]<br /><applet load="1i17" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1i17" />
'''NMR STRUCTURE OF MOUSE DOPPEL 51-157'''<br />


==Overview==
==NMR STRUCTURE OF MOUSE DOPPEL 51-157==
The downstream prion-like protein (doppel, or Dpl) is a paralog of the, cellular prion protein, PrP(C). The two proteins have approximately 25%, sequence identity, but seem to have distinct physiologic roles. Unlike, PrP(C), Dpl does not support prion replication; instead, overexpression of, Dpl in the brain seems to cause a completely different neurodegenerative, disease. We report the solution structure of a fragment of recombinant, mouse Dpl (residues 26-157) containing a globular domain with three, helices and a small amount of beta-structure. Overall, the topology of Dpl, is very similar to that of PrP(C). Significant differences include a, marked kink in one of the helices in Dpl, and a different orientation of, the two short beta-strands. Although the two proteins most likely arose, through duplication of a single ancestral gene, the relationship is now so, distant that only the structures retain similarity; the functions have, diversified along with the sequence.
<StructureSection load='1i17' size='340' side='right'caption='[[1i17]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I17 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1i17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i17 OCA], [https://pdbe.org/1i17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i17 RCSB], [https://www.ebi.ac.uk/pdbsum/1i17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i17 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRND_MOUSE PRND_MOUSE]
== 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/i1/1i17_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1i17 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The downstream prion-like protein (doppel, or Dpl) is a paralog of the cellular prion protein, PrP(C). The two proteins have approximately 25% sequence identity, but seem to have distinct physiologic roles. Unlike PrP(C), Dpl does not support prion replication; instead, overexpression of Dpl in the brain seems to cause a completely different neurodegenerative disease. We report the solution structure of a fragment of recombinant mouse Dpl (residues 26-157) containing a globular domain with three helices and a small amount of beta-structure. Overall, the topology of Dpl is very similar to that of PrP(C). Significant differences include a marked kink in one of the helices in Dpl, and a different orientation of the two short beta-strands. Although the two proteins most likely arose through duplication of a single ancestral gene, the relationship is now so distant that only the structures retain similarity; the functions have diversified along with the sequence.


==About this Structure==
Two different neurodegenerative diseases caused by proteins with similar structures.,Mo H, Moore RC, Cohen FE, Westaway D, Prusiner SB, Wright PE, Dyson HJ Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2352-7. PMID:11226243<ref>PMID:11226243</ref>
1I17 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I17 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Two different neurodegenerative diseases caused by proteins with similar structures., Mo H, Moore RC, Cohen FE, Westaway D, Prusiner SB, Wright PE, Dyson HJ, Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2352-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11226243 11226243]
</div>
<div class="pdbe-citations 1i17" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Cohen FE]]
[[Category: Cohen, F.E.]]
[[Category: Dyson HJ]]
[[Category: Dyson, H.J.]]
[[Category: Mo H]]
[[Category: Mo, H.]]
[[Category: Moore RC]]
[[Category: Moore, R.C.]]
[[Category: Prusiner SB]]
[[Category: Prusiner, S.B.]]
[[Category: Westaway D]]
[[Category: Westaway, D.]]
[[Category: Wright PE]]
[[Category: Wright, P.E.]]
[[Category: doppel]]
[[Category: dpl]]
[[Category: mouse doppel]]
[[Category: prion]]
 
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