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

Lignende værker

• Mutations at Beta N265 in γ-Aminobutyric Acid Type A Receptors Alter Both Binding Affinity and Efficacy of Potent Anesthetics
  af: Stewart, Deirdre S., et al.
  Udgivet: (2014)
• Alphaxalone Binds in Inner Transmembrane β(+)–α(−) Interfaces of α1β3γ2 γ-Aminobutyric Acid Type A Receptors
  af: Ziemba, Alexis M., et al.
  Udgivet: (2018)
• Monod-Wyman-Changeux Allosteric Shift Analysis in Mutant α1β3γ2L GABA(A) Receptors Indicates Selectivity and Crosstalk among Intersubunit Transmembrane Anesthetic Sites
  af: Szabo, Andrea, et al.
  Udgivet: (2019)
• Cysteine Substitutions Define Etomidate Binding and Gating Linkages in the α-M1 Domain of γ-Aminobutyric Acid Type A (GABA(A)) Receptors
  af: Stewart, Deirdre S., et al.
  Udgivet: (2013)
• State-Dependent Etomidate Occupancy of Its Allosteric Agonist Sites Measured in a Cysteine-Substituted GABA(A) Receptor
  af: Stewart, Deirdre S., et al.
  Udgivet: (2013)