3HER

Human prion protein variant F198S with V129

3HER の概要

• エントリーDOI: 10.2210/pdb3her/pdb
• 関連するPDBエントリー: 3HAF 3HAK 3HEQ 3HES
• 分子名称: Major prion protein, CADMIUM ION (3 entities in total)
• 機能のキーワード: prion protein, cell membrane, disease mutation, disulfide bond, glycoprotein, golgi apparatus, gpi-anchor, lipoprotein, membrane, polymorphism, prion, membrane protein
• 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: 2
• 化学式量合計: 32378.49

構造登録者

Lee, S.,Antony, L.,Hartmann, R.,Knaus, K.J.,Surewicz, K.,Surewicz, W.K.,Yee, V.C. (登録日: 2009-05-10, 公開日: 2010-01-12, 最終更新日: 2024-11-20)

主引用文献

Lee, S.,Antony, L.,Hartmann, R.,Knaus, K.J.,Surewicz, K.,Surewicz, W.K.,Yee, V.C.
Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.
Embo J., 29:251-262, 2010

PubMed Abstract: A conformational transition of normal cellular prion protein (PrP(C)) to its pathogenic form (PrP(Sc)) is believed to be a central event in the transmission of the devastating neurological diseases known as spongiform encephalopathies. The common methionine/valine polymorphism at residue 129 in the PrP influences disease susceptibility and phenotype. We report here seven crystal structures of human PrP variants: three of wild-type (WT) PrP containing V129, and four of the familial variants D178N and F198S, containing either M129 or V129. Comparison of these structures with each other and with previously published WT PrP structures containing M129 revealed that only WT PrPs were found to crystallize as domain-swapped dimers or closed monomers; the four mutant PrPs crystallized as non-swapped dimers. Three of the four mutant PrPs aligned to form intermolecular beta-sheets. Several regions of structural variability were identified, and analysis of their conformations provides an explanation for the structural features, which can influence the formation and conformation of intermolecular beta-sheets involving the M/V129 polymorphic residue.

PubMed: 19927125
DOI: 10.1038/emboj.2009.333

実験手法

X-RAY DIFFRACTION (1.85 Å)