Doppel - Revision history

Kurt Giles at 04:27, 22 December 2008

2008-12-22T04:27:52Z

← Older revision		Revision as of 04:27, 22 December 2008
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	==Structure of Dpl==		==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>		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>

Eran Hodis at 14:25, 15 December 2008

2008-12-15T14:25:13Z

← Older revision		Revision as of 14:25, 15 December 2008
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	{{STRUCTURE_1lg4 \| PDB=1lg4 \| SCENE= }}		{{STRUCTURE_1lg4 \| PDB=1lg4 \| SCENE= }}
	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 [[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.

	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>		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>

Eran Hodis at 14:24, 15 December 2008

2008-12-15T14:24:56Z

← Older revision		Revision as of 14:24, 15 December 2008
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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 of Dpl==

Eran Hodis at 14:24, 15 December 2008

2008-12-15T14:24:34Z

← Older revision		Revision as of 14:24, 15 December 2008
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	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 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.

	The structure mutant PrP with the additional disulphide bond was also ~~determoned~~ <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>		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>

Kurt Giles at 09:21, 15 December 2008

2008-12-15T09:21:36Z

← Older revision		Revision as of 09:21, 15 December 2008
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	==References==		==References==
	<~~reference~~/>		<references/>

Kurt Giles at 09:21, 15 December 2008

2008-12-15T09:21:18Z

← Older revision		Revision as of 09:21, 15 December 2008
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	==References==		==References==
	</~~reference~~>		<reference/>

Kurt Giles at 09:20, 15 December 2008

2008-12-15T09:20:03Z

← Older revision		Revision as of 09:20, 15 December 2008
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	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 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.

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


	=Related structures=		==Related structures==
	* [[1z65]] Mouse Dpl residues 1-30		* [[1z65]] Mouse Dpl residues 1-30
	* [[1lg4]] Human Dpl residues 24-152		* [[1lg4]] Human Dpl residues 24-152
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	=References=		==References==
	</reference>		</reference>

Kurt Giles at 09:18, 15 December 2008

2008-12-15T09:18:50Z

← Older revision		Revision as of 09:18, 15 December 2008
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	Doppel (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein like''<ref>1</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 of Dpl==

	{{STRUCTURE_1lg4 \| PDB=1lg4 \| SCENE= }}		{{STRUCTURE_1lg4 \| PDB=1lg4 \| SCENE= }}
	Dpl has the same fold as PrP, with three alpha helices and two short beta strands, 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 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.

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


	=Related structures=		=Related structures=
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	=References=		=References=
	~~{{Reflist}}~~		</reference>
	~~Moore ''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~~ </reference>
	~~Zahn R. et al. (2003) NMR structure of a variant human prion protein with two disulfide bridges'' J. Mol. Biol.'' '''326''', 225-34.~~

Kurt Giles at 12:23, 14 December 2008

2008-12-14T12:23:01Z

← Older revision		Revision as of 12:23, 14 December 2008
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	{{STRUCTURE_1lg4 \| PDB=1lg4 \| SCENE= }}		{{STRUCTURE_1lg4 \| PDB=1lg4 \| SCENE= }}
	Dpl has the same fold as PrP, with three alpha helices and two short beta strands, 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 PrP, with three alpha helices and two short beta strands, however it differs in that the third helix has a significant kink in it and it also contains two disulphide bonds.

			=Related structures=
			* [[1z65]] Mouse Dpl residues 1-30
			* [[1lg4]] Human Dpl residues 24-152
			* [[1i17]] Mouse Dpl residues 51-157
			* [[1h0l]] Human PrP residues 121-230, with an additional disulphide bond analogous to the homolog [[Doppel]]


	=References=		=References=
			{{Reflist}}
	Moore ''et al.'' (1999) Ataxia in Prion Protein (PrP)-deficient Mice is		Moore ''et al.'' (1999) Ataxia in Prion Protein (PrP)-deficient Mice is
	Associated with Upregulation of the Novel PrP-like		Associated with Upregulation of the Novel PrP-like
	Protein Doppel ''J. Mol. Biol.'' '''292''', 797-817		Protein Doppel ''J. Mol. Biol.'' '''292''', 797-817 </reference>
			Zahn R. et al. (2003) NMR structure of a variant human prion protein with two disulfide bridges'' J. Mol. Biol.'' '''326''', 225-34.

Kurt Giles: New page: Doppel (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein like''1, is a homolog of the prion protein (PrP). It is a cell surface glycoprotein. ==Structure of Dpl...

2008-12-14T12:01:02Z

New page: Doppel (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein like''<ref>1</ref>, is a homolog of the prion protein (PrP). It is a cell surface glycoprotein. ==Structure of Dpl...

New page

Doppel (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein like''<ref>1</ref>, is a homolog of the [[prion protein]] (PrP). It is a cell surface glycoprotein.

==Structure of Dpl==

{{STRUCTURE_1lg4 | PDB=1lg4 | SCENE= }}
Dpl has the same fold as PrP, with three alpha helices and two short beta strands, however it differs in that the third helix has a significant kink in it and it also contains two disulphide bonds.

=References=

Moore ''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