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Altered Protein Structure was Found in Autism Patients

ligin fails to properly align at synapses helps explain why the autism spectrum disorders are manifested in subtle behavioral abnormalities that are seen at an early age.

Abnormal synaptic development in nerve connections is likely to lead to cognitive deficits seen in patients with autism, said Taylor. He added that synapse formation and maintenance occurs early in development when the infant brain is still plastic and formative. Therefore, by understanding the structural mutations that affect neurotransmission during development, new leads into drug therapies may emerge.

We really dont know what causes autism, but this research represents a solid starting point, said Sarah Dunsmore, Ph.D., program director with the National Institute of General Medical Sciences, part of the National Institutes of Health, which partly supported the study. The work suggests that genetic mutations that alter the shape or folding of adhesion proteins in the nervous system influence their interactions. This is another example of how research on basic biological questions, such as the three-dimensional structures of proteins in the brain, can yield valuable medical insights.

Taylor and colleagues have been studying the structure and function of acetylcholinesterase a structurally related protein that mediates neurotransmission between nerves and between nerve and muscle for the past 30 years. They began studying the neuroligins because of the similarity in structure and amino acid sequence with acetylcholinesterase.


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