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  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.

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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

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Neuron_17_1996_343.pdf (Any fulltext), 541KB
 
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 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              

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 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

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Language(s): eng - English
 Dates: 1996-05-061996-08-01
 Publication Status: Published in print
 Pages: -
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 Rev. Type: Peer
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Title: Neuron
Source Genre: Journal
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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