Article
Exploring the cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis.
Proteins - 1 Jul 2017
Srinivasan E, Rajasekaran R
Abstract excerpt
Amyotrophic lateral sclerosis (ALS), a lethal neurodegenerative disorder is characterized by the degeneration of upper and lower motor neuron. ALS occurs due to various notably prominent missense mutations, in gene encoding Cu-Zn superoxide dismutase (SOD1) thereby leading to aggregation, dysfunction and reduced Zn binding affinity. In this study, one such mutation, G85R was explored in comparison with wild type...
Topics
- Amino Acid Substitution
- Amyotrophic Lateral Sclerosis
- Arginine
- Binding Sites
- Glycine
- Humans
- Molecular Dynamics Simulation
- Mutation
- Protein Aggregates
- Protein Binding
- Protein Conformation, alpha-Helical
- Protein Conformation, beta-Strand
- Protein Folding
- Protein Interaction Domains and Motifs
- Superoxide Dismutase-1
- Zinc