1QLZ

Human prion protein

1QLZ の概要

• エントリーDOI: 10.2210/pdb1qlz/pdb
• 関連するPDBエントリー: 1AG2 1QLX 1QM0 1QM1 1QM2 1QM3
• 分子名称: PRION PROTEIN (1 entity in total)
• 機能のキーワード: prion protein, prion, brain, glycoprotein, gpi-anchor, polymorphism, disease mutation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22922.21

構造登録者

Zahn, R.,Liu, A.,Luhrs, T.,Wuthrich, K. (登録日: 1999-09-20, 公開日: 1999-12-16, 最終更新日: 2024-11-06)

主引用文献

Zahn, R.,Liu, A.,Luhrs, T.,Riek, R.,Von Schroetter, C.,Garcia, F.L.,Billeter, M.,Calzolai, L.,Wider, G.,Wuthrich, K.
NMR Solution Structure of the Human Prion Protein
Proc.Natl.Acad.Sci.USA, 97:145-, 2000

PubMed Abstract: The NMR structures of the recombinant human prion protein, hPrP(23-230), and two C-terminal fragments, hPrP(90-230) and hPrP(121-230), include a globular domain extending from residues 125-228, for which a detailed structure was obtained, and an N-terminal flexibly disordered "tail." The globular domain contains three alpha-helices comprising the residues 144-154, 173-194, and 200-228 and a short anti-parallel beta-sheet comprising the residues 128-131 and 161-164. Within the globular domain, three polypeptide segments show increased structural disorder: i.e., a loop of residues 167-171, the residues 187-194 at the end of helix 2, and the residues 219-228 in the C-terminal part of helix 3. The local conformational state of the polypeptide segments 187-193 in helix 2 and 219-226 in helix 3 is measurably influenced by the length of the N-terminal tail, with the helical states being most highly populated in hPrP(23-230). When compared with the previously reported structures of the murine and Syrian hamster prion proteins, the length of helix 3 coincides more closely with that in the Syrian hamster protein whereas the disordered loop 167-171 is shared with murine PrP. These species variations of local structure are in a surface area of the cellular form of PrP that has previously been implicated in intermolecular interactions related both to the species barrier for infectious transmission of prion disease and to immune reactions.

PubMed: 10618385
DOI: 10.1073/PNAS.97.1.145

実験手法

SOLUTION NMR