5j48

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==PKG I's Carboyl Terminal Cyclic Nucleotide Binding Domain (CNB-B) in a complex with 8-pCPT-cGMP==
==PKG I's Carboyl Terminal Cyclic Nucleotide Binding Domain (CNB-B) in a complex with 8-pCPT-cGMP==
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<StructureSection load='5j48' size='340' side='right' caption='[[5j48]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
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<StructureSection load='5j48' size='340' side='right'caption='[[5j48]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5j48]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J48 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5j48]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J48 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6FW:2-AMINO-8-[(4-CHLOROPHENYL)SULFANYL]-9-[(2S,4AR,6R,7R,7AS)-2,7-DIHYDROXY-2-OXOTETRAHYDRO-2H,4H-2LAMBDA~5~-FURO[3,2-D][1,3,2]DIOXAPHOSPHININ-6-YL]-3,9-DIHYDRO-6H-PURIN-6-ONE'>6FW</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.12 2.7.11.12] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6FW:2-AMINO-8-[(4-CHLOROPHENYL)SULFANYL]-9-[(2S,4AR,6R,7R,7AS)-2,7-DIHYDROXY-2-OXOTETRAHYDRO-2H,4H-2LAMBDA~5~-FURO[3,2-D][1,3,2]DIOXAPHOSPHININ-6-YL]-3,9-DIHYDRO-6H-PURIN-6-ONE'>6FW</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5j48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j48 OCA], [http://pdbe.org/5j48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j48 RCSB], [http://www.ebi.ac.uk/pdbsum/5j48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j48 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5j48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j48 OCA], [https://pdbe.org/5j48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j48 RCSB], [https://www.ebi.ac.uk/pdbsum/5j48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j48 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KGP1_HUMAN KGP1_HUMAN]] Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle.<ref>PMID:8182057</ref> <ref>PMID:10567269</ref> <ref>PMID:11162591</ref> <ref>PMID:12082086</ref> <ref>PMID:11723116</ref> <ref>PMID:14608379</ref> <ref>PMID:15194681</ref> <ref>PMID:16990611</ref> <ref>PMID:21402151</ref>
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[https://www.uniprot.org/uniprot/KGP1_HUMAN KGP1_HUMAN] Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle.<ref>PMID:8182057</ref> <ref>PMID:10567269</ref> <ref>PMID:11162591</ref> <ref>PMID:12082086</ref> <ref>PMID:11723116</ref> <ref>PMID:14608379</ref> <ref>PMID:15194681</ref> <ref>PMID:16990611</ref> <ref>PMID:21402151</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Transferase]]
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[[Category: Homo sapiens]]
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[[Category: Campbell, J C]]
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[[Category: Large Structures]]
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[[Category: Kim, C W]]
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[[Category: Campbell JC]]
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[[Category: Sankaran, B]]
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[[Category: Kim CW]]
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[[Category: Analog]]
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[[Category: Sankaran B]]
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[[Category: Binding site]]
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[[Category: Cyclic amp]]
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[[Category: Cyclic gmp]]
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[[Category: Cyclic gmp-dependent protein kinase type ii]]
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[[Category: Mutagenesis]]
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[[Category: Protein binding]]
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[[Category: Site-directed]]
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Current revision

PKG I's Carboyl Terminal Cyclic Nucleotide Binding Domain (CNB-B) in a complex with 8-pCPT-cGMP

PDB ID 5j48

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OCA

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