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Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters
The structure of a bacterial homologue of these transporters from Aquifex aeolicus, in complex with its substrate, leucine, and two sodium ions, is presented and reveals the architecture of this important class of transporter, illuminates the determinants of substrate binding and ion selectivity, and defines the external and internal gates.
Principles of activation and permeation in an anion-selective Cys-loop receptor
The first three-dimensional structure, to the authors' knowledge, of an inhibitory anion-selective Cys-loop receptor, the homopentameric Caenorhabditis elegans glutamate-gated chloride channel α (GluCl), is presented at 3.3 Å resolution.
Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH.
Between the acidic residues and the transmembrane pore lies a disulphide-rich 'thumb' domain poised to couple the binding of protons to the opening of the ion channel, thus demonstrating that proton activation involves long-range conformational changes.
X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
The crystal structure of the α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor is reported at 3.6 Å resolution in complex with a competitive antagonist to exploit mechanisms of ion channel activation, desensitization and inhibition by non-competitive antagonists and pore blockers.
Structure of a glutamate transporter homologue from Pyrococcus horikoshii
This work presents the crystal structure of a eukaryotic glutamate transporter homologue from Pyrococcus horikoshii and proposes that transport of glutamate is achieved by movements of the hairpins that allow alternating access to either side of the membrane.
Crystal structure of the ATP-gated P2X4 ion channel in the closed state
This work defines the location of three non-canonical, intersubunit ATP-binding sites, and suggests that ATP binding promotes subunit rearrangement and ion channel opening.
Molecular mechanism of ATP binding and ion channel activation in P2X receptors
The structural delineation of the ATP-binding site and the ion channel pore, together with the conformational changes associated with ion channel gating, will stimulate development of new pharmacological agents.
Mechanism of glutamate receptor desensitization
Using the GluR2 AMPA-sensitive glutamate receptor, it is shown that the ligand-binding cores form dimers and that stabilization of the intradimer interface by either mutations or allosteric modulators reduces desensitization.
Mechanisms for Activation and Antagonism of an AMPA-Sensitive Glutamate Receptor Crystal Structures of the GluR2 Ligand Binding Core
Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
Secondary transporters are integral membrane proteins that catalyse the movement of substrate molecules across the lipid bilayer by coupling substrate transport to one or more ion gradients, thereby…