1I17
NMR STRUCTURE OF MOUSE DOPPEL 51-157
Summary for 1I17
| Entry DOI | 10.2210/pdb1i17/pdb |
| NMR Information | BMRB: 4938 |
| Descriptor | PRION-LIKE PROTEIN (1 entity in total) |
| Functional Keywords | mouse doppel, doppel, dpl, prion, unknown function |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 12297.79 |
| Authors | Mo, H.,Moore, R.C.,Cohen, F.E.,Westaway, D.,Prusiner, S.B.,Wright, P.E.,Dyson, H.J. (deposition date: 2001-01-31, release date: 2001-03-07, Last modification date: 2024-10-30) |
| Primary citation | Mo, H.,Moore, R.C.,Cohen, F.E.,Westaway, D.,Prusiner, S.B.,Wright, P.E.,Dyson, H.J. Two different neurodegenerative diseases caused by proteins with similar structures. Proc.Natl.Acad.Sci.USA, 98:2352-2357, 2001 Cited by PubMed Abstract: 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. PubMed: 11226243DOI: 10.1073/pnas.051627998 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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