A Cysteine Substitution Probes β3H267 Interactions with Propofol and Other Potent Anesthetics in α1β3γ2L γ-Aminobutyric Acid Type A Receptors.

ABSTRACT:

Background

Anesthetic contact residues in γ-aminobutyric acid type A (GABAA) receptors have been identified using photolabels, including two propofol derivatives. O-propofol diazirine labels H267 in β3 and α1β3 receptors, whereas m-azi-propofol labels other residues in intersubunit clefts of α1β3. Neither label has been studied in αβγ receptors, the most common isoform in mammalian brain. In αβγ receptors, other anesthetic derivatives photolabel m-azi-propofol-labeled residues, but not βH267. The authors' structural homology model of α1β3γ2L receptors suggests that β3H267 may abut some of these sites.

Methods

Substituted cysteine modification-protection was used to test β3H267C interactions with four potent anesthetics: propofol, etomidate, alphaxalone, and R-5-allyl-1-methy

SUBMITTER: Stern AT 

PROVIDER: S-EPMC4681607 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature