2WYT

1.0 A resolution structure of L38V SOD1 mutant

2WYT の概要

• エントリーDOI: 10.2210/pdb2wyt/pdb
• 関連するPDBエントリー: 1AZV 1BA9 1DSW 1FUN 1HL4 1HL5 1KMG 1L3N 1MFM 1N18 1N19 1OEZ 1OZT 1OZU 1P1V 1PTZ 1PU0 1RK7 1SOS 1SPD 1UXL 1UXM 2AF2 2C9S 2C9U 2C9V 2V0A 2VR6 2VR7 2VR8 2WKO 2WYZ 2WZ0 4SOD
• 分子名称: SUPEROXIDE DISMUTASE [CU-ZN], COPPER (II) ION, ZINC ION, ... (7 entities in total)
• 機能のキーワード: oxidoreductase, disease mutation, amyotrophic lateral sclerosis, antioxidant
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm : P00441
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32722.12

構造登録者

Antonyuk, S.V.,Strange, R.W.,Hasnain, S.S. (登録日: 2009-11-20, 公開日: 2010-10-27, 最終更新日: 2024-11-13)

主引用文献

Antonyuk, S.V.,Strange, R.W.,Hasnain, S.S.
Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights for Lead Optimization.
J.Med.Chem., 53:1402-, 2010

PubMed Abstract: Dominant inheritance of point mutations in CuZn superoxide dismutase (SOD1) is the best characterized subset of familial amyotrophic lateral sclerosis (FALS) and accounts for some 20% of the known familial cases. We report the discovery and visualization via cocrystallography of two ligand-binding pockets in human SOD1 and its pathogenic mutants that have opened up the real possibility of undertaking lead compound discovery using a fragment-based approach for therapeutic purposes for SOD1 associated motor neuron disease.

PubMed: 20067275
DOI: 10.1021/JM9017948

実験手法

X-RAY DIFFRACTION (1 Å)