Doppel
From Proteopedia
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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>. | + | 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> | ||
Current revision
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 the C-terminal domain PrP, with three alpha helices and two short beta strands[2]. However Dpl differs from PrP in two important respects: the second helix of Dpl has a pronounced kink in it, and Dpl also contains .
The structure mutant PrP with the additional disulphide bond was also determined [3]
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
- ↑ 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
- ↑ Mo H et al. (2001) Proc. Natl. Acad. Sci. USA 98,2352-7
- ↑ Zahn R et al. (2003) NMR structure of a variant human prion protein with two disulfide bridges J. Mol. Biol. 326, 225-34.
