|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='5c8w' size='340' side='right'caption='[[5c8w]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5c8w' size='340' side='right'caption='[[5c8w]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c8w]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C8W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c8w]] is a 6 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=5C8W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C8W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRKG2, PRKGR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr> |
| - | <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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5c8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c8w OCA], [https://pdbe.org/5c8w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c8w RCSB], [https://www.ebi.ac.uk/pdbsum/5c8w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c8w ProSAT]</span></td></tr> |
| - | <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=5c8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c8w OCA], [http://pdbe.org/5c8w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c8w RCSB], [http://www.ebi.ac.uk/pdbsum/5c8w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c8w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/KGP2_HUMAN KGP2_HUMAN] |
| - | Membrane-bound cGMP-dependent protein kinase (PKG) II is a key regulator of bone growth, renin secretion, and memory formation. Despite its crucial physiological roles, little is known about its cyclic nucleotide selectivity mechanism due to a lack of structural information. Here, we find that the C-terminal cyclic nucleotide binding (CNB-B) domain of PKG II binds cGMP with higher affinity and selectivity, compared to its N-terminal CNB (CNB-A) domain. To understand the structural basis of cGMP selectivity, we solved co-crystal structures of the CNB domains with cyclic nucleotides. Our structures combined with mutagenesis demonstrate that the guanine specific contacts at D412 and R415 of the alphaC-helix of CNB-B are crucial for cGMP selectivity and activation of PKG II. Structural comparison with the cGMP selective CNB domains of human PKG I and Plasmodium falciparum PKG (PfPKG) shows different contacts with the guanine moiety, revealing a unique cGMP selectivity mechanism for PKG II.
| + | |
| - | | + | |
| - | Structural Basis of Cyclic Nucleotide Selectivity in cGMP-Dependent Protein Kinase II.,Campbell JC, Kim JJ, Li KY, Huang GY, Reger AS, Matsuda S, Sankaran B, Link TM, Yuasa K, Ladbury JE, Casteel DE, Kim C J Biol Chem. 2016 Jan 14. pii: jbc.M115.691303. PMID:26769964<ref>PMID:26769964</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5c8w" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Transferase]]
| + | [[Category: Campbell JC]] |
| - | [[Category: Campbell, J C]] | + | [[Category: Huang GY]] |
| - | [[Category: Huang, G Y]] | + | [[Category: Kim CW]] |
| - | [[Category: Kim, C W]] | + | [[Category: Kim JJ]] |
| - | [[Category: Kim, J J]] | + | [[Category: Reger AS]] |
| - | [[Category: Reger, A S]] | + | [[Category: Sankaran B]] |
| - | [[Category: Sankaran, B]] | + | |
| - | [[Category: Binding site]]
| + | |
| - | [[Category: Cyclic amp]]
| + | |
| - | [[Category: Cyclic gmp]]
| + | |
| - | [[Category: Cyclic gmp-dependent protein kinase type ii]]
| + | |
| - | [[Category: Mutagenesis]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Site-directed]]
| + | |
