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Human members of the solute carrier 1 (SLC1) family of transporters take up excitatory neurotransmitters in the brain, mainly glutamate, and amino acids in peripheral organs. Dysregulation of their functions… Click to show full abstract
Human members of the solute carrier 1 (SLC1) family of transporters take up excitatory neurotransmitters in the brain, mainly glutamate, and amino acids in peripheral organs. Dysregulation of their functions is associated to neurodegenerative disorders and cancer. Here we present recent high-resolution structural and dynamic data obtained from a thermostable human glutamate transporter. In particular, combining X-ray crystallography and hydrogen-deuterium exchange mass spectrometry, we have now revealed architectural features of human SLC1 proteins and a novel allosteric mechanism of transport inhibition, opening new venues for drug design targeting SLC1 transporters.
Journal Title: Biophysical Journal
Year Published: 2017
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