Anesthesiology December 2016 PMID 27753644

Tryptophan and Cysteine Mutations in M1 Helices of α1β3γ2L γ-Aminobutyric Acid Type A Receptors Indicate Distinct Intersubunit Sites for Four Intravenous Anesthetics and One Orphan Site.

Anahita Nourmahnad, Alex T Stern, Mayo Hotta, Deirdre S Stewart, Alexis M Ziemba, Andrea Szabo, Stuart A Forman

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Abstract in brief

It identifies specific amino acids, such as 1M236 and 3M227, as key contact points influenced by these anesthetics, with mutations causing spontaneous channel gating and altering receptor sensitivity.
Different mutational strategies, including tryptophan substitutions and cysteine modifications, revealed distinct and overlapping binding sites within the receptor's intersubunit pockets, showing how anesthetic binding affects receptor function and gating behavior, with protections observed at certain residues like 1L232C and 3M227C.
These findings suggest that each anesthetic may target varied but overlapping sites, contributing to their allosteric effects on the receptor.
Overall, the results demonstrate that all five transmembrane pockets of GABAA receptors are functionally linked to channel gating and that anesthetic interactions at specific residues within these pockets modulate receptor activity, providing insight into the molecular basis of anesthetic action and highlighting potential sites for drug development.
Notably, no protection was observed at some residues, like 2I242C or 2L246C, indicating selective binding sites for different anesthetics.

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Mapping Binding Sites of General Anesthetics on GABAA Receptors

The study investigates how intravenous anesthetics like etomidate, propofol, barbiturates, and neurosteroids interact with GABAA receptor subunits, identifying key amino acids and distinct intersubunit binding sites…

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