3jbq
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PDE5A_BOVIN PDE5A_BOVIN] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP (PubMed:8530505). Specifically regulates nitric-oxide-generated cGMP (By similarity).[UniProtKB:O76074]<ref>PMID:8530505</ref> [https://www.uniprot.org/uniprot/PDE6C_BOVIN PDE6C_BOVIN] As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellular levels of cGMP.[UniProtKB:P51160] | [https://www.uniprot.org/uniprot/PDE5A_BOVIN PDE5A_BOVIN] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP (PubMed:8530505). Specifically regulates nitric-oxide-generated cGMP (By similarity).[UniProtKB:O76074]<ref>PMID:8530505</ref> [https://www.uniprot.org/uniprot/PDE6C_BOVIN PDE6C_BOVIN] As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellular levels of cGMP.[UniProtKB:P51160] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The cGMP phosphodiesterase of rod photoreceptor cells, PDE6, is the key effector enzyme in phototransduction. Two large catalytic subunits, PDE6alpha and -beta, each contain one catalytic domain and two non-catalytic GAF domains, whereas two small inhibitory PDE6gamma 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 approximately 11 A 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/delta) indicated the location of the PDE6 C-terminal prenylations. Reconstructions of complexes with Fab fragments bound to N or C termini of PDE6gamma revealed that PDE6gamma stretches from the catalytic domain at one end of the holoenzyme to the GAF-A domain at the other. Removal of PDE6gamma caused dramatic structural rearrangements, which were reversed upon its restoration. | ||
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| + | Domain Organization and Conformational Plasticity of the G Protein Effector, PDE6.,Zhang Z, He F, Constantine R, Baker ML, Baehr W, Schmid MF, Wensel TG, Agosto MA J Biol Chem. 2015 May 15;290(20):12833-43. doi: 10.1074/jbc.M115.647636. Epub, 2015 Mar 25. PMID:25809480<ref>PMID:25809480</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3jbq" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Domain Organization and Conformational Plasticity of the G Protein Effector, PDE6
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Categories: Bos taurus | Large Structures | Mus musculus | Agosto MA | Baehr W | Baker ML | Constantine R | He F | Schmid MF | Wensel TG | Zhang Z
