Doppel: Difference between revisions

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Doppel (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein-like''<ref>Moore, R ''et al.'' (1999) Ataxia in Prion Protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein Doppel ''J. Mol. Biol.'' '''292''', 797-817</ref>, is a homolog of the [[prion protein]] (PrP). It is a cell surface glycoprotein.

[[Doppel]] (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein-like''<ref>Moore, R ''et al.'' (1999) Ataxia in Prion Protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein Doppel ''J. Mol. Biol.'' '''292''', 797-817</ref>, is a homolog of the [[prion protein]] (PrP). It is a cell surface glycoprotein.

==Structure of Dpl==

Dpl has the same fold as PrP, with three alpha helices and two short beta strands<ref>Mo H ''et al.'' (2001) ''Proc. Natl. Acad. Sci. USA'' '''98''',2352-7</ref>. ~~however it~~ differs in ~~that~~ the ~~third~~ helix has a ~~significant~~ kink in it and it also contains two disulphide bonds.

Dpl has the same fold as the C-terminal domain [[PrP]], with three alpha helices and two short beta strands<ref>Mo H ''et al.'' (2001) ''Proc. Natl. Acad. Sci. USA'' '''98''',2352-7</ref>. However Dpl differs from [[PrP]] in two important respects: the second helix of Dpl has a pronounced kink in it, and Dpl also contains <scene name='Doppel/Disulfide_bonds/1'>two disulphide bonds</scene>.

The structure mutant PrP with the additional disulphide bond was also determined <ref>Zahn R ''et al.'' (2003) NMR structure of a variant human prion protein with two disulfide bridges '' J. Mol. Biol.'' '''326''', 225-34.</ref>

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-Doppel (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein-like''<ref>Moore, R ''et al.'' (1999) Ataxia in Prion Protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein Doppel ''J. Mol. Biol.'' '''292''', 797-817</ref>, is a homolog of the [[prion protein]] (PrP). It is a cell surface glycoprotein.
+[[Doppel]] (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein-like''<ref>Moore, R ''et al.'' (1999) Ataxia in Prion Protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein Doppel ''J. Mol. Biol.'' '''292''', 797-817</ref>, is a homolog of the [[prion protein]] (PrP). It is a cell surface glycoprotein.
 ==Structure of Dpl==
-{{STRUCTURE_1lg4 |  PDB=1lg4  |  SCENE=  }}
+{{STRUCTURE_1lg4 |  PDB=1lg4  |  SCENE=Doppel/Cartoon/1  }}
-Dpl has the same fold as PrP, with three alpha helices and two short beta strands<ref>Mo H ''et al.'' (2001) ''Proc. Natl. Acad. Sci. USA'' '''98''',2352-7</ref>.  however it differs in that the third helix has a significant kink in it and it also contains two disulphide bonds.
+Dpl has the same fold as the C-terminal domain [[PrP]], with three alpha helices and two short beta strands<ref>Mo H ''et al.'' (2001) ''Proc. Natl. Acad. Sci. USA'' '''98''',2352-7</ref>.  However Dpl differs from [[PrP]] in two important respects: the second helix of Dpl has a pronounced kink in it, and Dpl also contains <scene name='Doppel/Disulfide_bonds/1'>two disulphide bonds</scene>.
 The structure mutant PrP with the additional disulphide bond was also determined <ref>Zahn R ''et al.'' (2003) NMR structure of a variant human prion protein with two disulfide bridges '' J. Mol. Biol.'' '''326''', 225-34.</ref>