Doppel: Difference between revisions

Latest revision as of 07:27, 22 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 DplStructure of Dpl

1lg4, 20 NMR models ()

Gene:

Prnd (Homo sapiens)

Related:

1i17

Structural annotation:
Resources:	CATH : 1Lg4A00 InterPro : Ipr000817 Pfam : PF00377 SCOP : d1lg4a_ UniProt : Q9UKY0

Functional annotation:
Cellular component:	membrane
Biological process:	protein homooligomerization
Molecular function:	GPI anchor binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

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 structuresRelated 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

ReferencesReferences

↑ 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.

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Kurt Giles, Eran Hodis

[1] 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

[2] Mo H et al. (2001) Proc. Natl. Acad. Sci. USA 98,2352-7

[3] Zahn R et al. (2003) NMR structure of a variant human prion protein with two disulfide bridges J. Mol. Biol. 326, 225-34.

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 ==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>.  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 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>