Agonist- and antagonist-induced conformational changes of loop F and their contributions to the rho1 GABA receptor function.

@article{Zhang2009AgonistAA,
  title={Agonist- and antagonist-induced conformational changes of loop F and their contributions to the rho1 GABA receptor function.},
  author={Jianliang Zhang and Fenqin Xue and Y. N. Chang},
  journal={The Journal of physiology},
  year={2009},
  volume={587 1},
  pages={
          139-53
        }
}
Binding of gamma-aminobutyric acid (GABA) to its receptor initiates a conformational change to open the channel, but the mechanism of the channel activation is not well understood. To this end, we scanned loop F (K210-F227) in the N-terminal domain of the rho1 GABA receptor expressed in Xenopus oocytes using a site-specific fluorescence technique. We detected GABA-induced fluorescence changes at six positions (K210, K211, L216, K217, T218 and I222). At these positions the fluorescence changes… CONTINUE READING
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