English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Polyamine spider toxins and NMDA receptors: structural basis for channel block and binding of argiotoxin636

Raditsch, M., Geyer, M., Kalbitzer, H. R., Ruppersberg, J. P., Jahn, W., & Witzemann, V. (1996). Polyamine spider toxins and NMDA receptors: structural basis for channel block and binding of argiotoxin636. European Journal of Biochemistry, 240, 416-426. Retrieved from http://www.ejbiochem.org/cgi/content/abstract/240/2/416?maxtoshow%3D%26HITS%3D10%26hits%3D10%26RESULTFORMAT%3D%26searchid%3D1021620596745_21%26stored_search%3D%26FIRSTINDEX%3D0%26volume%3D240%26firstpage%3D416%26fdate%3D1%2F1%2F1996%26tdate%3D12%2F31%2F1996%26journalcode%3Dejbiochem%3A.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Polyamine spider toxins and NMDA receptors: structural basis for channel block and binding of argiotoxin636

Files

show Files
hide Files
:
EurJBiochem_240_1996_416.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
EurJBiochem_240_1996_416.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Raditsch, Martin1, Author           
Geyer, Matthias2, Author           
Kalbitzer, Hans Robert2, Author           
Ruppersberg, J. Peter1, Author           
Jahn, Werner2, Author           
Witzemann, Veit1, 3, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
3Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

Content

show
hide
Free keywords: -
 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 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

Details

show
hide
Language(s): eng - English
 Dates: 1996-06-131996-02-261996-09
 Publication Status: Issued
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: European Journal of Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 240 Sequence Number: - Start / End Page: 416 - 426 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040