1B10

SOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION PROTEIN RPRP(90-231) , 25 STRUCTURES

「2PRP」から置き換えられました

1B10 の概要

• エントリーDOI: 10.2210/pdb1b10/pdb
• 分子名称: PROTEIN (PRION PROTEIN) (1 entity in total)
• 機能のキーワード: prion, scrapie, brain, glycoprotein, prion protein
• 由来する生物種: Mesocricetus auratus (golden hamster)
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04273
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16264.10

構造登録者

James, T.L.,Liu, H.,Ulyanov, N.B.,Farr-Jones, S. (登録日: 1998-11-25, 公開日: 1998-12-02, 最終更新日: 2024-11-06)

主引用文献

James, T.L.,Liu, H.,Ulyanov, N.B.,Farr-Jones, S.,Zhang, H.,Donne, D.G.,Kaneko, K.,Groth, D.,Mehlhorn, I.,Prusiner, S.B.,Cohen, F.E.
Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.
Proc.Natl.Acad.Sci.USA, 94:10086-10091, 1997

PubMed Abstract: The scrapie prion protein (PrPSc) is the major, and possibly the only, component of the infectious prion; it is generated from the cellular isoform (PrPC) by a conformational change. N-terminal truncation of PrPSc by limited proteolysis produces a protein of approximately 142 residues designated PrP 27-30, which retains infectivity. A recombinant protein (rPrP) corresponding to Syrian hamster PrP 27-30 was expressed in Escherichia coli and purified. After refolding rPrP into an alpha-helical form resembling PrPC, the structure was solved by multidimensional heteronuclear NMR, revealing many structural features of rPrP that were not found in two shorter PrP fragments studied previously. Extensive side-chain interactions for residues 113-125 characterize a hydrophobic cluster, which packs against an irregular beta-sheet, whereas residues 90-112 exhibit little defined structure. Although identifiable secondary structure is largely lacking in the N terminus of rPrP, paradoxically this N terminus increases the amount of secondary structure in the remainder of rPrP. The surface of a long helix (residues 200-227) and a structured loop (residues 165-171) form a discontinuous epitope for binding of a protein that facilitates PrPSc formation. Polymorphic residues within this epitope seem to modulate susceptibility of sheep and humans to prion disease. Conformational heterogeneity of rPrP at the N terminus may be key to the transformation of PrPC into PrPSc, whereas the discontinuous epitope near the C terminus controls this transition.

PubMed: 9294167
DOI: 10.1073/pnas.94.19.10086

実験手法

SOLUTION NMR