The role of Loop F in the activation of the GABA receptor

Alpa Khatri, David S. Weiss

Research output: Contribution to journalReview articlepeer-review

14 Scopus citations

Abstract

Functional studies of the ligand gated ion channel family (nicotinic acetylcholine, serotonin Type 3, glycine and GABA receptors) along with the crystal structure of the acetylcholine binding protein (AChBP) and molecular dynamics simulations of the nAChR structure have resulted in a structural model in which the agonist-binding pocket comprises six loops (A-F) contributed by adjacent subunits. It is presumed that the binding of agonist results in a local structural rearrangement that is then transduced to the gate, causing the pore to open. Efforts are underway to better define the specific roles of the six binding loops. Several studies have suggested Loop F may play a direct role in linking the structural rearrangement within the binding pocket to the gate, although other investigations have indicated Loop F may be crucial for locking the agonist molecule into the binding site. This review will focus on the controversy surrounding the role of Loop F during GABA receptor activation.

Original languageEnglish (US)
Pages (from-to)59-66
Number of pages8
JournalJournal of Physiology
Volume588
Issue number1
DOIs
StatePublished - Jan 2010

ASJC Scopus subject areas

  • Physiology

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