The catalytic and GAF domains of the rod cGMP phosphodiesterase (PDE6) heterodimer are regulated by distinct regions of its inhibitory γ subunit
H Mou, RH Cote - Journal of Biological Chemistry, 2001 - ASBMB
The central effector of visual transduction in retinal rod photoreceptors, cGMP
phosphodiesterase (PDE6), is a catalytic heterodimer (αβ) to which low molecular weight
inhibitory γ subunits bind to form the nonactivated PDE holoenzyme (αβγ 2). Although it is
known that γ binds tightly to αβ, the binding affinity for each γ subunit to αβ, the domains on γ
that interact with αβ, and the allosteric interactions between γ and the regulatory and
catalytic regions on αβ are not well understood. We show here that the γ subunit binds to two …
phosphodiesterase (PDE6), is a catalytic heterodimer (αβ) to which low molecular weight
inhibitory γ subunits bind to form the nonactivated PDE holoenzyme (αβγ 2). Although it is
known that γ binds tightly to αβ, the binding affinity for each γ subunit to αβ, the domains on γ
that interact with αβ, and the allosteric interactions between γ and the regulatory and
catalytic regions on αβ are not well understood. We show here that the γ subunit binds to two …
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