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          Institute: MPI für medizinische Forschung     Collection: Max-Planck-Forschungsgruppe Ionenkanalstruktur (Dean R. Madden)     Display Documents

ID: 22918.0, MPI für medizinische Forschung / Max-Planck-Forschungsgruppe Ionenkanalstruktur (Dean R. Madden)
Large-scale expression and thermodynamic characterization of a glutamate receptor agonist-binding domain
Translation of Title:Large-scale expression and thermodynamic characterization of a glutamate receptor agonist-binding domain
Authors:Madden, Dean R.; Abele, Rupert; Andersson, Arnold; Keinänen, Kari
Date of Publication (YYYY-MM-DD):2000-07
Title of Journal:European Journal of Biochemistry
Journal Abbrev.:Eur. J. Biochem.
Issue / Number:13
Start Page:4281
End Page:4289
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:The ionotropic glutamate receptors (GluR) are the primary mediators of excitatory synaptic transmission in the brain. GluR agonist binding has been localized to an extracellular domain whose core is homologous to the bacterial periplasmic binding proteins (PBP). We have established routine, baculovirus-mediated expression of a complete ligand-binding domain construct at the 10-L scale, yielding 10-40 milligrams of purified protein. This construct contains peptides that lie outside the PBP-homologous core and that connect the domain core to the transmembrane domains of the channel and to the N-terminal X-domain. These linker peptides have been implicated in modulating channel physiology. Such extended constructs have proven difficult to express in bacteria, but the protein described here is stable and monomeric. Isothermal titration calorimetry reveals that glutamate binding to the domain involves a substantial heat capacity change and that at physiological temperatures, the reaction is both entropically and enthalpically favorable. Glutamate receptor ion channels (GluR) are responsible for most excitatory synaptic communication in the central nervous system. They play an important role in the regulation of synaptic strength and are involved in a number of neuropathological processes, including post-traumatic neuronal damage, epilepsy and neurodegenerative diseases. GluR can be divided into three subclasses based on their pharmacological selectivity for the agonists alpha-amino-5-methyl-3-hydroxy-4-isoxazole propionate (AMPA), kainate and N-methyl- d-aspartate (NMDA) (reviewed in [ 1]). Like many ion channels, the GluR exhibit desensitization [ 2], the kinetics and extent of which depend on the agonist used.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Nachwuchsgruppe Ion Channel Structure/
Identifiers:URI: [Full text]
URI: [Abstract]
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