1I17

NMR STRUCTURE OF MOUSE DOPPEL 51-157

1I17 の概要

• エントリーDOI: 10.2210/pdb1i17/pdb
• NMR情報: BMRB: 4938
• 分子名称: PRION-LIKE PROTEIN (1 entity in total)
• 機能のキーワード: mouse doppel, doppel, dpl, prion, unknown function
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12297.79

構造登録者

Mo, H.,Moore, R.C.,Cohen, F.E.,Westaway, D.,Prusiner, S.B.,Wright, P.E.,Dyson, H.J. (登録日: 2001-01-31, 公開日: 2001-03-07, 最終更新日: 2024-10-30)

主引用文献

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

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: 11226243
DOI: 10.1073/pnas.051627998

実験手法

SOLUTION NMR