Pharmacology of structural changes at the GABA(A) receptor transmitter binding site.

ABSTRACT:

Background and purpose

The binding of transmitter to specialized binding pockets leads to rearrangements in the structure of the receptor eventually resulting in channel opening. We used voltage-clamp fluorometry to investigate the pharmacological basis and biophysical processes that underlie structural changes at the transmitter binding site of the rat α1β2γ2L GABA(A) receptor.

Experimental approach

Simultaneous electrophysiological and site-specific fluorescence measurements were conducted on receptors expressed in Xenopus oocytes and labelled with an environmentally-sensitive fluorophore, Alexa 546 maleimide, at the α1L127C site.

Key results

Receptors activated by GABA demonstrate a concentration-dependent increase in fluorescence intensity, indicating that the env

SUBMITTER: Akk G 

PROVIDER: S-EPMC3042195 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature