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

  • Kuner T
  • Wollmuth L
  • Karlin A
 et al. 
  • 57

    Readers

    Mendeley users who have this article in their library.
  • 184

    Citations

    Citations of this article.

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 α-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.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Thomas KunerHeidelberg University

    Follow
  • Lonnie P. Wollmuth

  • Arthur Karlin

  • Peter H. Seeburg

  • Bert Sakmann

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free