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Article

Assessment of ligand binding at a site relevant to SOD1 oxidation and aggregation.

FEBS letters - 1 May 2018

Manjula Ramu, Wright Gareth S A, Strange Richard W, Padmanabhan Balasundaram

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 29679384
DOI: 10.1002/1873-3468.13055

Genes

SOD1

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