Doppel: Difference between revisions
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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 | ||
| Line 16: | Line 16: | ||
=References= | ==References== | ||
</reference> | </reference> | ||
Revision as of 09:20, 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 (default scene) | |||||||||||||
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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]
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
</reference>
- ↑ 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.
