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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"  
[[Image:1i17.gif|left|200px]]<br /><applet load="1i17" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1i17" />
caption="1i17" />
'''NMR STRUCTURE OF MOUSE DOPPEL 51-157'''<br />
'''NMR STRUCTURE OF MOUSE DOPPEL 51-157'''<br />


==Overview==
==Overview==
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.
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==
==About this Structure==
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].  
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://oca.weizmann.ac.il/oca-bin/ocashort?id=1I17 OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cohen, F.E.]]
[[Category: Cohen, F E.]]
[[Category: Dyson, H.J.]]
[[Category: Dyson, H J.]]
[[Category: Mo, H.]]
[[Category: Mo, H.]]
[[Category: Moore, R.C.]]
[[Category: Moore, R C.]]
[[Category: Prusiner, S.B.]]
[[Category: Prusiner, S B.]]
[[Category: Westaway, D.]]
[[Category: Westaway, D.]]
[[Category: Wright, P.E.]]
[[Category: Wright, P E.]]
[[Category: doppel]]
[[Category: doppel]]
[[Category: dpl]]
[[Category: dpl]]
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[[Category: prion]]
[[Category: prion]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:57:59 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:53 2008''