3LTV

Mouse-human sod1 chimera

3LTV の概要

• エントリーDOI: 10.2210/pdb3ltv/pdb
• 関連するPDBエントリー: 3GTT 3GTV
• 分子名称: Superoxide dismutase [Cu-Zn],Superoxide dismutase [Cu-Zn], ZINC ION (3 entities in total)
• 機能のキーワード: oxidoreductase, antioxidant, metal-binding, amyotrophic lateral sclerosis, disease mutation, phosphoprotein
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Cytoplasm : P00441
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 94894.54

構造登録者

Seetharaman, S.V.,Taylor, A.B.,Hart, P.J. (登録日: 2010-02-16, 公開日: 2010-09-08, 最終更新日: 2024-11-20)

主引用文献

Seetharaman, S.V.,Taylor, A.B.,Holloway, S.,Hart, P.J.
Structures of mouse SOD1 and human/mouse SOD1 chimeras.
Arch.Biochem.Biophys., 503:183-190, 2010

PubMed Abstract: Mutations in human copper-zinc superoxide dismutase (SOD1) cause an inherited form of amyotrophic lateral sclerosis (ALS). Inclusions enriched in pathogenic SOD1 accumulate in the spinal cords of transgenic mice expressing these proteins, but endogenous mouse SOD1 is not found as a component of these aggregates. In the accompanying paper, Karch and colleagues analyze aggregation propensities of human/mouse SOD1 chimeras in cell culture and identify two sequence elements in the human enzyme that seem to enhance its aggregation relative to the mouse enzyme. Here, we report the first structure of mouse SOD1 along with those of SOD1 chimeras in which residues 1-80 come from human SOD1 and residues 81-153 come from mouse SOD1 and vice versa. Taken together, the structural and cell-based data suggest a model in which residues Q42 and Q123 in mouse SOD1 modulate non-native SOD1-SOD1 intermolecular interactions at edge strands in the SOD1 Greek key β-barrel.

PubMed: 20727846
DOI: 10.1016/j.abb.2010.08.014

実験手法

X-RAY DIFFRACTION (2.453 Å)