Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange.

@article{Ahmed2013DynamicsOC,
  title={Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange.},
  author={Ahmed R H Ahmed and Christopher P Ptak and Michael K. Fenwick and Ching-Lin Hsieh and Gregory A. Weiland and Robert E. Oswald},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 38},
  pages={
          27658-66
        }
}
The majority of excitatory neurotransmission in the CNS is mediated by tetrameric AMPA receptors. Channel activation begins with a series of interactions with an agonist that binds to the cleft between the two lobes of the ligand-binding domain of each subunit. Binding leads to a series of conformational transitions, including the closure of the two lobes of the binding domain around the ligand, culminating in ion channel opening. Although a great deal has been learned from crystal structures… CONTINUE READING
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