English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structural determinants of ion flow through recombinant glutamate receptor channels

Verdoorn, T. A., Burnashev, N., Monyer, H., Seeburg, P. H., & Sakmann, B. (1991). Structural determinants of ion flow through recombinant glutamate receptor channels. Science, 252(5013), 1715-1718. doi:10.1126/science.1710829.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-ACBA-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-70B4-6
Genre: Journal Article

Files

show Files
hide Files
:
Science_252_1991_1715.pdf (Any fulltext), 972KB
 
File Permalink:
-
Name:
Science_252_1991_1715.pdf
Description:
-
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:
-
Locator:
https://doi.org/10.1126/science.1710829 (Any fulltext)
Description:
-

Creators

show
hide
 Creators:
Verdoorn, Todd A., Author
Burnashev, Nail1, Author              
Monyer, Hannah2, Author              
Seeburg, Peter H.2, Author              
Sakmann, Bert1, Author              
Affiliations:
1Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              
2Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

Content

show
hide
Free keywords: -
 Abstract: Functional glutamate receptor (GluRs) were transiently expressed in cultured mammalian cells from cloned complementary DNAs encoding GluR-A, -B, -C, or -D polypeptides. The steady-state current-voltage (I-V) relations of glutamate- and kainate-induced currents through homomeric channels fell into two classes: channels composed of either the GluR-A, -C, and -D subunits showed doubly rectifying I-V curves, and channels composed of the GluR-B subunits displayed simple outward rectification. The presence of GluR-B subunits in heteromeric GluRs determined the I-V behavior of the resulting channels. Site-directed mutagenesis identified a single amino acid difference (glutamine to arginine) in the putative transmembrane segment TM2 responsible for subunit-specific I-V relationships. The properties of heteromeric wild-type and mutant GluRs revealed that the dominance of GluR-B is due to the arginine residue in the TM2 region.

Details

show
hide
Language(s): eng - English
 Dates: 1991-03-081991-04-301991-06-21
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.1710829
URI: 10.1126/science.1710829
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Science
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 252 (5013) Sequence Number: - Start / End Page: 1715 - 1718 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1