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          Institute: MPI für medizinische Forschung     Collection: Abteilung Zellphysiologie     Display Documents



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ID: 23243.0, MPI für medizinische Forschung / Abteilung Zellphysiologie
Polyamine spider toxins and NMDA receptors: Structural basis for channel block and binding of argiotoxin636
Translation of Title:Polyamine spider toxins and NMDA receptors: Structural basis for channel block and binding of argiotoxin636
Authors:Raditsch, Martin; Geyer, Matthias; Kalbitzer, Hans Robert; Ruppersberg, J. Peter; Jahn, Werner; Witzemann, Veit
Language:English
Date of Publication (YYYY-MM-DD):1996
Title of Journal:European Journal of Biochemistry
Journal Abbrev.:Eur. J. Biochem.
Volume:240
Start Page:416
End Page:426
Copyright:© 1996 by Federation of European Biochemical Societies
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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 brain membranes, in contrast, reveal no specific binding or yield binding constants which differ by orders of magnitude from the IC50 values of the functional assays. One explanation is that argiotoxin636 does not bind with high affinity to the inhibitory site in the N-methyl-D-aspartate-receptor channel under in vitro conditions when membranes are depolarised. The structure of argiotoxin636 was investigated by NMR spectroscopy. In solution the positively charged argiotoxin636 acquires an extended conformation and its dimensions might allow permeation deep into the channel. In the absence of direct structural information on the channel protein, the detailed analysis of blockade in conjunction with structural information, as provided here, may be of aid in the deduction of structural features of glutamate-receptor channel ion pores.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Zellphysiologie
Relations:-URI:http://www.jphysiol.org/cgi/content/full/509/3/635
Identifiers:URI:http://www.ejbiochem.org/cgi/content/abstract/240/... [Abstract]
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