PMID: 8938723Jan 1, 1996Paper

Time resolved kinetics of direct G beta 1 gamma 2 interactions with the carboxyl terminus of Kir3.4 inward rectifier K+ channel subunits

Neuropharmacology
C A DoupnikH A Lester

Abstract

The direct interaction of recombinant G beta 1 gamma 2 proteins with the carboxyl terminal domain of a G protein-gated inward rectifier K channel subunit, Kir3.4 (GIRK4), was measured in real time using biosensor chip technology. The carboxyl terminus of Kir3.4 (a.a. 186-419) was expressed in bacteria as a glutathione-S-transferase (GST) fusion protein, GST-Kir3. 4ct. GST-Kir3.4ct was immobilized to the surface of a biosensor chip by high affinity binding of the GST domain to a covalently attached anti-GST antibody. The association and dissociation rates of G beta 1 gamma 2 dimers with the immobilized Kir3.4ct domain were temporally resolved as a change in refractive index detected by surface plasmon resonance. Specific binding of G beta 1 gamma 2 dimers to Kir3.4ct was characterized by a dissociation rate (kd) of approximately 0.003 s-1. Association kinetics were dominated by a concentration-independent component (time constant approximately 50 s) which complicates models of binding and may indicate conformational changes during binding of G beta 1 gamma 2 to Kir3.4ct. The estimated equilibrium dissociation binding constant (Kd) was approximately 800 nM. These studies demonstrate that G beta gamma dimers interact directly with...Continue Reading

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Citations

Jul 9, 1999·Journal of Molecular Recognition : JMR·A HuberD Neri
Mar 12, 2004·Brain Research. Developmental Brain Research·Marcus H AndrewsStephen G Matthews
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