English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines

Kuner, T., Wollmuth, L. P., Karlin, A., Seeburg, P. H., & Sakmann, B. (1996). Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines. Neuron, 17, 343-352. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/8780657.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-2254-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-2255-6
Genre: Journal Article
Alternative Title : Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines

Files

show Files
hide Files
:
Neuron_17_1996_343.pdf (Any fulltext), 541KB
 
File Permalink:
-
Name:
Neuron_17_1996_343.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Kuner, Thomas1, 2, Author              
Wollmuth, Lonnie P.2, Author              
Karlin, Arthur, Author
Seeburg, Peter H.1, Author              
Sakmann, Bert2, Author              
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

Content

show
hide
Free keywords: -
 Abstract: The structure of the NMDA receptor channel M2 segment was investigated by probing the extracellular and cytoplasmic faces of cysteine−substituted NR1?NR2C channels with charged sulfhydryl−specific reagents. The pattern of accessible positions suggests that the M2 segment forms a channel−lining loop originating and ending on the cytoplasmic side of the channel, with the ascending limb in an ?−helical structure and the descending limb in an extended structure. A functionally critical asparagine (N−site) is positioned at the tip of the loop, and a cluster of hydrophilic residues of the descending limb, adjacent to the tip, forms the narrow constriction of the channel. An apparent asymmetric positioning of the NR1− and NR2−subunit N−site asparagines may account for their unequal role in Ca2+ permeability and Mg2+ block

Details

show
hide
Language(s): eng - English
 Dates: 1996-05-061996-08-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Neuron
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 17 Sequence Number: - Start / End Page: 343 - 352 Identifier: ISSN: 0896-6273
CoNE: https://pure.mpg.de/cone/journals/resource/954925560565