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Polyamine spider toxins and mammalian N-methyl-D-aspartate receptors. Structural basis for channel blocking and binding of argiotoxin₆₃₆

Raditsch, M. and Geyer, M. and Kalbitzer, Hans Robert and Jahn, W. and Ruppersberg, J .P. and Witzemann, V. (1996) Polyamine spider toxins and mammalian N-methyl-D-aspartate receptors. Structural basis for channel blocking and binding of argiotoxin₆₃₆. European journal of biochemistry = the FEBS journal 240 (2), pp. 416-426.

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Abstract

Recombinant N-methyl-D-aspartate receptors composed of NR1/NR2A subunits were expressed in Xenopus oocytes to analyse the voltage-dependent and use-dependent channel blocking activity of argiotoxin636. Functional assays demonstrate that the toxin competes with other open channel blockers such as Mg2+ and MK-801. Direct binding or competition assays using radiolabeled ligands and isolated rat ...

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Item Type:Article
Date:1996
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
8841407PubMed ID
Classification:
NotationType
AnimalsMESH
Binding, CompetitiveMESH
Brain/metabolismMESH
Cell Membrane/metabolismMESH
Dizocilpine Maleate/pharmacologyMESH
Excitatory Amino Acid Antagonists/pharmacologyMESH
Hydrogen-Ion ConcentrationMESH
Ion Channels/antagonists & inhibitorsMESH
Magnesium/metabolismMESH
Magnetic Resonance SpectroscopyMESH
Models, MolecularMESH
Molecular StructureMESH
Oocytes/metabolismMESH
Patch-Clamp TechniquesMESH
Phenylacetates/pharmacologyMESH
Polyamines/pharmacologyMESH
RatsMESH
Receptors, N-Methyl-D-Aspartate/metabolismMESH
Recombinant Proteins/metabolismMESH
Spider VenomsMESH
XenopusMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:09 Sep 2010 06:36
Last Modified:09 Sep 2010 06:36
Item ID:16542
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