English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons93934

Kuner,  Thomas
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95979

Wollmuth,  Lonnie P.
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95292

Seeburg,  Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95089

Sakmann,  Bert
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-2254-8
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