1i17

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i17 OCA], [http://www.ebi.ac.uk/pdbsum/1i17 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i17 RCSB]</span>
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[[Category: prion]]
[[Category: prion]]
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Revision as of 18:13, 30 March 2008


PDB ID 1i17

Drag the structure with the mouse to rotate
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NMR STRUCTURE OF MOUSE DOPPEL 51-157


Overview

The downstream prion-like protein (doppel, or Dpl) is a paralog of the cellular prion protein, PrP(C). The two proteins have approximately 25% sequence identity, but seem to have distinct physiologic roles. Unlike PrP(C), Dpl does not support prion replication; instead, overexpression of Dpl in the brain seems to cause a completely different neurodegenerative disease. We report the solution structure of a fragment of recombinant mouse Dpl (residues 26-157) containing a globular domain with three helices and a small amount of beta-structure. Overall, the topology of Dpl is very similar to that of PrP(C). Significant differences include a marked kink in one of the helices in Dpl, and a different orientation of the two short beta-strands. Although the two proteins most likely arose through duplication of a single ancestral gene, the relationship is now so distant that only the structures retain similarity; the functions have diversified along with the sequence.

About this Structure

1I17 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Two different neurodegenerative diseases caused by proteins with similar structures., Mo H, Moore RC, Cohen FE, Westaway D, Prusiner SB, Wright PE, Dyson HJ, Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2352-7. PMID:11226243

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