5yv9 - Revision history

OCA at 08:38, 22 November 2023

2023-11-22T08:38:38Z

←Older revision		Revision as of 08:38, 22 November 2023
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	<StructureSection load='5yv9' size='340' side='right'caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>		<StructureSection load='5yv9' size='340' side='right'caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5yv9]] is a 1 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=5YV9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5YV9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5yv9]] 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=5YV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YV9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=91O:5-chloro-2-methoxy-4[(1Z)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]aminobenzoic+acid'>91O</scene>, <scene name='pdbligand=CL:~~CHLORIDE+ION~~'>CL</scene>, <scene name='pdbligand=~~GOL~~:~~GLYCEROL~~'>~~GOL~~</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]] 2.53Å</td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=~~CAS~~:~~S-(DIMETHYLARSENIC)CYSTEINE~~'>~~CAS~~</scene~~></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=91O:5-chloro-2-methoxy-4[(1Z)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]aminobenzoic+acid'>91O</scene>, <scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CAMKK2, CAMKKB, KIAA0787 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yv9 OCA], [https://pdbe.org/5yv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yv9 RCSB], [https://www.ebi.ac.uk/pdbsum/5yv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yv9 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yv9 OCA], [~~http~~://pdbe.org/5yv9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5yv9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5yv9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5yv9 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KKCC2_HUMAN KKCC2_HUMAN]] Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.<ref>PMID:11395482</ref> <ref>PMID:12935886</ref> <ref>PMID:9662074</ref> <ref>PMID:21957496</ref>	+	[https://www.uniprot.org/uniprot/KKCC2_HUMAN KKCC2_HUMAN] Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.<ref>PMID:11395482</ref> <ref>PMID:12935886</ref> <ref>PMID:9662074</ref> <ref>PMID:21957496</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5yv9" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5yv9" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Calcium/calmodulin-dependent protein kinase kinase\|Calcium/calmodulin-dependent protein kinase kinase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Calcium/calmodulin-dependent protein kinase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Handa, N]]	+	[[Category: Handa N]]
-	[[Category: Niwa, H]]	+	[[Category: Niwa H]]
-	[[Category: Yokoyama, S]]	+	[[Category: Yokoyama S]]
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Protein-inhibitor complex]]~~	+
-	~~[[Category: Serine/threonine-protein kinase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:31, 10 June 2020

2020-06-10T06:31:37Z

←Older revision		Revision as of 06:31, 10 June 2020
Line 1:		Line 1:

-	==Structure of CaMKK2~~-inhibitor~~ complex==	+	==Structure of CaMKK2 in complex with CKI-009==
	<StructureSection load='5yv9' size='340' side='right'caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>		<StructureSection load='5yv9' size='340' side='right'caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 05:55, 20 May 2020

2020-05-20T05:55:09Z

←Older revision		Revision as of 05:55, 20 May 2020
Line 3:		Line 3:
	<StructureSection load='5yv9' size='340' side='right'caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>		<StructureSection load='5yv9' size='340' side='right'caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5yv9]] is a 1 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=5YV9 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5YV9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5yv9]] is a 1 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=5YV9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YV9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=91O:5-chloro-2-methoxy-4[(1Z)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]aminobenzoic+acid'>91O</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=91O:5-chloro-2-methoxy-4[(1Z)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]aminobenzoic+acid'>91O</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CAMKK2, CAMKKB, KIAA0787 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CAMKK2, CAMKKB, KIAA0787 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </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=5yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yv9 OCA], [http://pdbe.org/5yv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yv9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yv9 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yv9 OCA], [http://pdbe.org/5yv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yv9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yv9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KKCC2_HUMAN KKCC2_HUMAN]] Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.<ref>PMID:11395482</ref> <ref>PMID:12935886</ref> <ref>PMID:9662074</ref> <ref>PMID:21957496</ref>		[[http://www.uniprot.org/uniprot/KKCC2_HUMAN KKCC2_HUMAN]] Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.<ref>PMID:11395482</ref> <ref>PMID:12935886</ref> <ref>PMID:9662074</ref> <ref>PMID:21957496</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	CaMKK2 (calcium/calmodulin dependent protein kinase kinase 2) is a serine/threonine protein kinase that regulates phosphorylation of CaM kinases (CaMKs) such as CaMKI, CaMKIV, and AMP-activated protein kinase (AMPK). From a pathological perspective, CaMKK2 plays a role in obesity, diabetes, and prostate cancer. Therefore, CaMKK2 is an attractive target protein for drug design. Here, we tried to find new CaMKK2 inhibitors by using ligand-based and structure-based drug design approaches. From the in silico hit compounds, we identified new inhibitors by using a CaMKK2 kinase assay. We solved X-ray crystallography structures of the CaMKK2-inhibitor complexes and performed Fragment Molecular Orbital (FMO) calculations to analyze the protein-ligand interactions, identify the key residues in inhibitor binding, and quantitatively measure their contribution. We experimentally determined five CaMKK2-inhibitor structures and calculated the binding energies of the inhibitors by the FMO method plus MM-PBSA (Molecular Mechanics Poisson-Boltzmann Surface Area) approach. The results showed a high correlation (R = -0.89) between experimentally measured inhibitory activity (pIC50) and the predicted ligand binding energy. We then quantitatively evaluated the contribution of each binding site residue in CaMKK2 by the IFIE (Inter-fragment Interaction Energy)/PIEDA (Pair Interaction Energy Decomposition Analysis) method. The IFIE values indicated that Lys194 and Glu236, which formed hydrogen bonds with the carboxylate groups of the inhibitors, were key residues for ligand binding. PIEDA revealed that the dispersion interaction of inhibitors with hydrophobic residues, such as Ile171, Phe267, and Leu319, contributed highly to ligand binding; we considered that this was due to CH-pi interactions with methoxy groups and/or aromatic rings contained in our CaMKK2 inhibitor. These results from the quantitative interaction analysis by the FMO method are useful not only for future CaMMK2 inhibitor development but for application of the FMO method to in silico drug design.
		+
		+	Protein ligand interaction analysis against new CaMKK2 inhibitors by use of X-ray crystallography and the fragment molecular orbital (FMO) method.,Takaya D, Niwa H, Mikuni J, Nakamura K, Handa N, Tanaka A, Yokoyama S, Honma T J Mol Graph Model. 2020 Apr 10;99:107599. doi: 10.1016/j.jmgm.2020.107599. PMID:32348940<ref>PMID:32348940</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5yv9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:23, 19 June 2019

2019-06-19T06:23:30Z

←Older revision		Revision as of 06:23, 19 June 2019
Line 1:		Line 1:

-	==~~A kinase~~-inhibitor complex==	+	==Structure of CaMKK2-inhibitor complex==
-	<StructureSection load='5yv9' size='340' side='right' caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>	+	<StructureSection load='5yv9' size='340' side='right'caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5yv9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YV9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YV9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5yv9]] is a 1 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=5YV9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YV9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=91O:5-chloro-2-methoxy-4[(1Z)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]aminobenzoic+acid'>91O</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=91O:5-chloro-2-methoxy-4[(1Z)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]aminobenzoic+acid'>91O</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CAMKK2, CAMKKB, KIAA0787 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </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=5yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yv9 OCA], [http://pdbe.org/5yv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yv9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yv9 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=5yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yv9 OCA], [http://pdbe.org/5yv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yv9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yv9 ProSAT]</span></td></tr>
Line 16:		Line 17:
	</StructureSection>		</StructureSection>
	[[Category: Calcium/calmodulin-dependent protein kinase]]		[[Category: Calcium/calmodulin-dependent protein kinase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Handa, N]]		[[Category: Handa, N]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]

OCA at 06:29, 5 December 2018

2018-12-05T06:29:04Z

←Older revision		Revision as of 06:29, 5 December 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5yv9 is ~~ON HOLD until Paper Publication~~	+	==A kinase-inhibitor complex==
-		+	<StructureSection load='5yv9' size='340' side='right' caption='[[5yv9]], [[Resolution\|resolution]] 2.53Å' scene=''>
-	~~Authors~~: ~~Niwa~~, H., ~~Handa~~, N., ~~Yokoyama~~, S.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5yv9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YV9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YV9 FirstGlance]. <br>
-	~~Description~~: A kinase-~~inhibitor complex~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=91O:5-chloro-2-methoxy-4[(1Z)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]aminobenzoic+acid'>91O</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </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=5yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yv9 OCA], [http://pdbe.org/5yv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yv9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yv9 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KKCC2_HUMAN KKCC2_HUMAN]] Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.<ref>PMID:11395482</ref> <ref>PMID:12935886</ref> <ref>PMID:9662074</ref> <ref>PMID:21957496</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Calcium/calmodulin-dependent protein kinase]]
	[[Category: Handa, N]]		[[Category: Handa, N]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]
	[[Category: Yokoyama, S]]		[[Category: Yokoyama, S]]
		+	[[Category: Atp-binding]]
		+	[[Category: Kinase]]
		+	[[Category: Protein-inhibitor complex]]
		+	[[Category: Serine/threonine-protein kinase]]
		+	[[Category: Transferase]]

OCA at 04:48, 20 December 2017

2017-12-20T04:48:59Z

←Older revision		Revision as of 04:48, 20 December 2017
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5yv9 is ON HOLD	+	The entry 5yv9 is ON HOLD until Paper Publication

	Authors: Niwa, H., Handa, N., Yokoyama, S.		Authors: Niwa, H., Handa, N., Yokoyama, S.

OCA: Protected "5yv9" [edit=sysop:move=sysop]

2017-11-29T05:01:35Z

Protected "5yv9" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:01, 29 November 2017

OCA: New page: '''Unreleased structure''' The entry 5yv9 is ON HOLD Authors: Niwa, H., Handa, N., Yokoyama, S. Description: A kinase-inhibitor complex Category: Unreleased Structures [[Category: ...

2017-11-29T05:01:34Z

New page: '''Unreleased structure''' The entry 5yv9 is ON HOLD Authors: Niwa, H., Handa, N., Yokoyama, S. Description: A kinase-inhibitor complex Category: Unreleased Structures [[Category: ...

New page

'''Unreleased structure'''

The entry 5yv9 is ON HOLD

Authors: Niwa, H., Handa, N., Yokoyama, S.

Description: A kinase-inhibitor complex
[[Category: Unreleased Structures]]
[[Category: Handa, N]]
[[Category: Niwa, H]]
[[Category: Yokoyama, S]]