Doppel

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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.
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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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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>
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=Related structures=
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==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=
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==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

PDB ID 1lg4

Drag the structure with the mouse to rotate
1lg4, 20 NMR models ()
Gene: Prnd (Homo sapiens)
Related: 1i17
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>

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Kurt Giles, Eran Hodis

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