Structural determinants of the PDE6 GAF A domain for binding the inhibitory γ-subunit and noncatalytic cGMP

Hakim MURADOV; Kimberly K BOYD; Nikolai O ARTEMYEV

doi:10.1016/j.visres.2004.05.013

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Structural determinants of the PDE6 GAF A domain for binding the inhibitory γ-subunit and noncatalytic cGMP

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Structural determinants of the PDE6 GAF A domain for binding the inhibitory γ-subunit and noncatalytic cGMP

Hakim MURADOV, Kimberly K BOYD and Nikolai O ARTEMYEV

Vision research (Oxford), Vol.44(21), pp.2437-2444

2004

DOI: 10.1016/j.visres.2004.05.013

PMID: 15358079

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Abstract

Photoreceptor cGMP phosphodiesterases (PDE6 family) are modular enzymes with each catalytic subunit containing two N-terminal regulatory GAF domains, GAF A and GAF B. The GAF A domains contribute to dimerization of the PDE6 catalytic subunits and to binding of the inhibitory Pgamma subunits, and represent candidate sites for noncatalytic binding of cGMP. We performed a mutational analysis of selected residues from the GAF A domain of cone PDEalpha' to identify the cGMP-binding pocket and delineate the Pgamma-binding surface. Results of this analysis establish the noncatalytic cGMP-binding site within the PDE6 GAF A domain and suggest that occupation of the pocket by cGMP is required for high-affinity binding of Pgamma to the proximate contact surface.

Cell Physiology

Fundamental and applied biological sciences. Psychology

Biological and medical sciences

Molecular and cellular biology

Vision, photoreception

Details

Title: Subtitle: Structural determinants of the PDE6 GAF A domain for binding the inhibitory γ-subunit and noncatalytic cGMP
Creators: Hakim MURADOV - Department of Physiology and Biophysics, University of Iowa College of Medicine, 5-532 Bowen Science Bldg. 51 Newton Road, Iowa City, IA 52242, United States
Kimberly K BOYD - Department of Physiology and Biophysics, University of Iowa College of Medicine, 5-532 Bowen Science Bldg. 51 Newton Road, Iowa City, IA 52242, United States
Nikolai O ARTEMYEV - Department of Physiology and Biophysics, University of Iowa College of Medicine, 5-532 Bowen Science Bldg. 51 Newton Road, Iowa City, IA 52242, United States
Resource Type: Journal article
Publication Details: Vision research (Oxford), Vol.44(21), pp.2437-2444
DOI: 10.1016/j.visres.2004.05.013
PMID: 15358079
NLM abbreviation: Vision Res
ISSN: 0042-6989
eISSN: 1878-5646
Publisher: Elsevier Science; Oxford
Language: English
Date published: 2004
Academic Unit: Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Ophthalmology and Visual Sciences
Record Identifier: 9984025327202771

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