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http://purl.uniprot.org/citations/25809480http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25809480http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25809480http://www.w3.org/2000/01/rdf-schema#comment"The cGMP phosphodiesterase of rod photoreceptor cells, PDE6, is the key effector enzyme in phototransduction. Two large catalytic subunits, PDE6α and -β, each contain one catalytic domain and two non-catalytic GAF domains, whereas two small inhibitory PDE6γ subunits allow tight regulation by the G protein transducin. The structure of holo-PDE6 in complex with the ROS-1 antibody Fab fragment was determined by cryo-electron microscopy. The ∼11 Å map revealed previously unseen features of PDE6, and each domain was readily fit with high resolution structures. A structure of PDE6 in complex with prenyl-binding protein (PrBP/δ) indicated the location of the PDE6 C-terminal prenylations. Reconstructions of complexes with Fab fragments bound to N or C termini of PDE6γ revealed that PDE6γ stretches from the catalytic domain at one end of the holoenzyme to the GAF-A domain at the other. Removal of PDE6γ caused dramatic structural rearrangements, which were reversed upon its restoration."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.org/dc/terms/identifier"doi:10.1074/jbc.M115.647636"xsd:string
http://purl.uniprot.org/citations/25809480http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m115.647636"xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Baker M.L."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Baker M.L."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"He F."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"He F."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Schmid M.F."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Schmid M.F."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Baehr W."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Baehr W."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Wensel T.G."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Wensel T.G."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Agosto M.A."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Agosto M.A."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Constantine R."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/author"Constantine R."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/25809480http://purl.uniprot.org/core/name"J Biol Chem"xsd:string