Structure of Altered Proteins Revealed in Autism Patients

A new research study, titled ¡°Structural Analysis of the Synaptic Protein Neuroligin and Its ¦Â-Neurexin Complex: Determinants for Folding and Cell Adhesion,¡± published online in the scientific journal Neuron, has described, at the atomic level, structural changes in altered proteins implicated in autism patients.

The study was led by Pascale Marchot, PhD, from the Institut F¨¦d¨¦ratif de Recherche Jean Roche, Universit¨¦ de la M¨¦diterran¨¦e, Facult¨¦ de M¨¦decine, Marseille, France. Colleagues form the Department of Pharmacology, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, CA participated in the study.

Researchers studied details of the neuroligin family of proteins, known to be mutated in autism disorders. The study found the specific mutations present in people with autism. They were able to identify the amino acids sequence that is mutated and where it is are located in the protein. They also show in their study how the folding of the protein is affected by this mutation.

Previously, the same researchers of this study were able to map the structure of the protein family of neuroligins and that of the related neurexins proteins. These two proteins are involved in the mechanism of transmission of the electrical impulse between neurons, that is, they are involved in the area of neuron-neuron interaction known as synapse.

Proteins are a polymer of amino acids. The specific sequence of amino acids in known as the primary structure of the protein. This primary structure determines the secondary structure (how they fold on 2 dimensions) and the tertiary structure (how they fold tridimensionally). The tertiary structure determines how the protein functions within the cell.