5YUL

Native Structure of hSOD1 in P6322 space group

5YUL の概要

• エントリーDOI: 10.2210/pdb5yul/pdb
• 分子名称: Superoxide dismutase [Cu-Zn], ZINC ION, Dihydrogen tetrasulfide, ... (5 entities in total)
• 機能のキーワード: dimer, native, oxidoreductase, dismutase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 160789.45

構造登録者

Manjula, R.,Padmanabhan, B. (登録日: 2017-11-22, 公開日: 2018-11-21, 最終更新日: 2024-11-13)

主引用文献

Manjula, R.,Wright, G.S.A.,Strange, R.W.,Padmanabhan, B.
Assessment of ligand binding at a site relevant to SOD1 oxidation and aggregation
FEBS Lett., 592:1725-1737, 2018

PubMed Abstract: Cu/Zn superoxide dismutase-1 (SOD1) mutations are causative for a subset of amyotrophic lateral sclerosis (ALS) cases. These mutations lead to structural instability, aggregation and ultimately motor neuron death. We have determined crystal structures of SOD1 in complex with a naphthalene-catechol-linked compound which binds with low micro-molar affinity to a site important for oxidative damage-induced aggregation. SOD1 Trp32 oxidation is indeed significantly inhibited by ligand binding. Our work shows how compound linking can be applied successfully to ligand interactions on the SOD1 surface to generate relatively good binding strength. The ligand, positioned in a region important for SOD1 fibrillation, offers the possibility that it, or a similar compound, could prevent the abnormal self-association that drives SOD1 toxicity in ALS.

PubMed: 29679384
DOI: 10.1002/1873-3468.13055

実験手法

X-RAY DIFFRACTION (1.9 Å)