Understanding the physiological processes involving transition metals with high redox activity such as copper or participant in many cellular functions such as zinc - both metalloenzyme present in the Cu, Zn-superoxide dismutase (SOD1 or Cu, Zn-SOD) - is becoming day more important to elucidate the molecular cause of some diseases. Many processes involving aggregation and function of SOD1 deleterious peroxidase is still in full discussion in the literature more than 40 years after its discovery and characterization. This area of research the role of mutations in the enzyme linked to familial cases of the disease Amyotrophic Lateral Sclerosis (ALS), a disease that particularly affects motor neurons, begins to be elucidated recently, where it was known that the type of protein aggregation observed and disease severity depends on the type of mutation in SOD1. Mutations affecting the zinc coordination mode are the most intriguing because reveal a highly pathogenic ALS. We know very little about how the SOD1 without mutations, would be involved in sporadic cases of ALS (most common). Our proposal is related to changes in the zinc binding site of the enzyme, leading to protein aggregation and aggressive forms of the disease.
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