Doppel
From Proteopedia
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| - | Doppel (Dpl), named for '''''do'''wnstream '''p'''rion '''p'''rotein like''<ref> | + | 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. |
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| + | 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. | ||
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=Related structures= | =Related structures= | ||
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=References= | =References= | ||
| - | + | </reference> | |
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Revision as of 09:18, 15 December 2008
Doppel (Dpl), named for downstream prion protein-like[1], is a homolog of the prion protein (PrP). It is a cell surface glycoprotein.
Structure of Dpl
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| 1lg4, 20 NMR models () | |||||||||
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| Gene: | Prnd (Homo sapiens) | ||||||||
| Related: | 1i17 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Dpl has the same fold as PrP, with three alpha helices and two short beta strands[2]. 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 [3]
