Doppel
From Proteopedia
(Difference between revisions)
(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...) |
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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= | ||
| + | {{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. | ||
Revision as of 12:23, 14 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, 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
- ↑ 1
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.
