5kjz

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==Co-crystal structure of PKA RI alpha CNB-B mutant (G316R/A336T) with cGMP==
==Co-crystal structure of PKA RI alpha CNB-B mutant (G316R/A336T) with cGMP==
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<StructureSection load='5kjz' size='340' side='right' caption='[[5kjz]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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<StructureSection load='5kjz' size='340' side='right'caption='[[5kjz]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kjz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KJZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kjz]] is a 1 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=5KJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KJZ 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</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]] 1.347&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kjy|5kjy]], [[5kjx|5kjx]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</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=5kjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjz OCA], [http://pdbe.org/5kjz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kjz RCSB], [http://www.ebi.ac.uk/pdbsum/5kjz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjz 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=5kjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjz OCA], [https://pdbe.org/5kjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kjz RCSB], [https://www.ebi.ac.uk/pdbsum/5kjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjz ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/KAP0_HUMAN KAP0_HUMAN]] Acute promyelocytic leukemia;Acrodysostosis with multiple hormone resistance;Familial atrial myxoma;Primary pigmented nodular adrenocortical disease;Carney complex;Acrodysostosis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/KAP0_HUMAN KAP0_HUMAN] Acute promyelocytic leukemia;Acrodysostosis with multiple hormone resistance;Familial atrial myxoma;Primary pigmented nodular adrenocortical disease;Carney complex;Acrodysostosis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KAP0_HUMAN KAP0_HUMAN]] Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.<ref>PMID:16491121</ref> <ref>PMID:20215566</ref> <ref>PMID:26405036</ref>
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[https://www.uniprot.org/uniprot/KAP0_HUMAN KAP0_HUMAN] Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.<ref>PMID:16491121</ref> <ref>PMID:20215566</ref> <ref>PMID:26405036</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyclic AMP and cyclic GMP are ubiquitous second messengers that regulate the activity of effector proteins in all forms of life. The main effector proteins, the 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) and the 3',5'-cyclic guanosine monophosphate (cGMP)-dependent protein kinase (PKG), are preferentially activated by cAMP and cGMP, respectively. However, the molecular basis of this cyclic nucleotide selectivity is still not fully understood. Analysis of isolated cyclic nucleotide-binding (CNB) domains of PKA regulatory subunit type Ialpha (RIalpha) reveals that the C-terminal CNB-B has a higher cAMP affinity and selectivity than the N-terminal CNB-A. Here, we show that introducing cGMP-specific residues using site-directed mutagenesis reduces the selectivity of CNB-B, while the combination of two mutations (G316R/A336T) results in a cGMP-selective binding domain. Furthermore, introducing the corresponding mutations (T192R/A212T) into the PKA RIalpha CNB-A turns this domain into a highly cGMP-selective domain, underlining the importance of these contacts for achieving cGMP specificity. Binding data with the generic purine nucleotide 3',5'-cyclic inosine monophosphate (cIMP) reveal that introduced arginine residues interact with the position 6 oxygen of the nucleobase. Co-crystal structures of an isolated CNB-B G316R/A336T double mutant with either cAMP or cGMP reveal that the introduced threonine and arginine residues maintain their conserved contacts as seen in PKG I CNB-B. These results improve our understanding of cyclic nucleotide binding and the molecular basis of cyclic nucleotide specificity.
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Mutations of PKA cyclic nucleotide-binding domains reveal novel aspects of cyclic nucleotide selectivity.,Lorenz R, Moon EW, Kim JJ, Schmidt SH, Sankaran B, Pavlidis IV, Kim C, Herberg FW Biochem J. 2017 Jul 6;474(14):2389-2403. doi: 10.1042/BCJ20160969. PMID:28583991<ref>PMID:28583991</ref>
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==See Also==
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*[[CAMP-dependent protein kinase 3D structures|CAMP-dependent protein kinase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5kjz" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Herberg, F W]]
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[[Category: Homo sapiens]]
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[[Category: Huang, G Y]]
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[[Category: Large Structures]]
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[[Category: Kim, C]]
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[[Category: Herberg FW]]
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[[Category: Kim, J J]]
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[[Category: Huang GY]]
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[[Category: Lorenz, R]]
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[[Category: Kim C]]
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[[Category: Moon, E]]
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[[Category: Kim JJ]]
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[[Category: Camp-dependent protein kinase]]
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[[Category: Lorenz R]]
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[[Category: Cyclic nucleotide]]
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[[Category: Moon E]]
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[[Category: Cyclic nucleotide binding domain]]
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[[Category: Nucleotide selectivity]]
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[[Category: Signaling protein]]
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Current revision

Co-crystal structure of PKA RI alpha CNB-B mutant (G316R/A336T) with cGMP

PDB ID 5kjz

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