The NMDA receptor M3 segment is a conserved transduction element coupling ligand binding to channel opening.

Published

Journal Article

Ion channels alternate stochastically between two functional states, open and closed. This gating behavior is controlled by membrane potential or by the binding of neurotransmitters in voltage- and ligand-gated channels, respectively. Although much progress has been made in defining the structure and function of the ligand-binding cores and the voltage sensors, how these domains couple to channel opening remains poorly understood. Here we show that the M3 transmembrane segments of the NMDA receptor allosterically interact with both the ligand-binding cores and the channel gate. It is proposed that M3 functions as a transduction element whose conformational change couples ligand binding with channel opening. Furthermore, amino acid homology between glutamate receptor M3 segments and the equivalent S6 or TM2 segments in K(+) channels suggests that ion channel activation and gating are both structurally and functionally conserved.

Full Text

Duke Authors

Cited Authors

  • Jones, KS; VanDongen, HMA; VanDongen, AMJ

Published Date

  • March 15, 2002

Published In

Volume / Issue

  • 22 / 6

Start / End Page

  • 2044 - 2053

PubMed ID

  • 11896144

Pubmed Central ID

  • 11896144

Electronic International Standard Serial Number (EISSN)

  • 1529-2401

Language

  • eng

Conference Location

  • United States