AMPA Receptor Ligand Binding Domain Mobility Revealed by Functional Cross Linking
نویسندگان
چکیده
منابع مشابه
AMPA receptor ligand binding domain mobility revealed by functional cross linking.
Glutamate receptors mediate the majority of excitatory synaptic transmission in the CNS. The AMPA-subtype has rapid kinetics, with activation, deactivation and desensitization proceeding on the millisecond timescale or faster. Crystallographic, biochemical, and functional studies suggest that GluR2 Cys mutants which form intermolecular disulfide cross-links between the lower D2 lobes of the lig...
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Transmembrane AMPA receptor (AMPAR) regulatory proteins (TARPs) markedly enhance AMPAR function, altering ligand efficacy and receptor gating kinetics and thereby shaping the postsynaptic response. The structural mechanism underlying TARP effects on gating, however, is unknown. Here we find that the prototypical member of the TARP family, stargazin or γ-2, rescues gating deficits in AMPARs carr...
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Academic Dissertation To be presented for public criticism, with the permission of the Faculty of Science of the (1998) Disulfide bonding and cysteine accessibility in the α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluRD. Implications for redox modulation of glutamate receptors. receptors and bacterial periplasmic amino acid-binding proteins share the ionic mechanism ...
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Ionotropic glutamate receptors are tetramers, the isolated ligand binding cores of which assemble as dimers. Previous work on nondesensitizing AMPA receptor mutants, which combined crystallography, ultracentrifugation, and patch-clamp recording, showed that dimer formation by the ligand binding cores is required for activation of ion channel gating by agonists. To define the mechanisms responsi...
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Desensitization of ionotropic glutamate receptors (GluRs), specifically the AMPA receptor subtype, shapes the postsynaptic response at certain synapses in the brain. All known mechanisms that alter desensitization, either pharmacological or mutational, are associated with the ligand-binding domain. Here we report that substitution of a conserved positively charged arginine (R) with a negatively...
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ژورنال
عنوان ژورنال: Journal of Neuroscience
سال: 2009
ISSN: 0270-6474,1529-2401
DOI: 10.1523/jneurosci.2971-09.2009