3a8w - Revision history

OCA at 16:19, 22 December 2021

OCA — Wed, 22 Dec 2021 16:19:50 GMT

←Older revision		Revision as of 16:19, 22 December 2021
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	<StructureSection load='3a8w' size='340' side='right'caption='[[3a8w]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3a8w' size='340' side='right'caption='[[3a8w]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3a8w]] is a 2 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=3A8W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3A8W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3a8w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A8W FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3a8v\|3a8v]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a8v\|3a8v]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Protein_kinase_C Protein kinase C], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.13 2.7.11.13] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_kinase_C Protein kinase C], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.13 2.7.11.13] </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=3a8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8w OCA], [~~http~~://pdbe.org/3a8w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3a8w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3a8w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8w ProSAT]</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=3a8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8w OCA], [https://pdbe.org/3a8w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a8w RCSB], [https://www.ebi.ac.uk/pdbsum/3a8w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/KPCI_HUMAN KPCI_HUMAN]] Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis.<ref>PMID:8226978</ref> <ref>PMID:9346882</ref> <ref>PMID:10467349</ref> <ref>PMID:10356400</ref> <ref>PMID:10906326</ref> <ref>PMID:11042363</ref> <ref>PMID:11724794</ref> <ref>PMID:12871960</ref> <ref>PMID:14684752</ref> <ref>PMID:15994303</ref> <ref>PMID:18270268</ref> <ref>PMID:19327373</ref> <ref>PMID:21419810</ref> <ref>PMID:21189248</ref>	+	[[https://www.uniprot.org/uniprot/KPCI_HUMAN KPCI_HUMAN]] Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis.<ref>PMID:8226978</ref> <ref>PMID:9346882</ref> <ref>PMID:10467349</ref> <ref>PMID:10356400</ref> <ref>PMID:10906326</ref> <ref>PMID:11042363</ref> <ref>PMID:11724794</ref> <ref>PMID:12871960</ref> <ref>PMID:14684752</ref> <ref>PMID:15994303</ref> <ref>PMID:18270268</ref> <ref>PMID:19327373</ref> <ref>PMID:21419810</ref> <ref>PMID:21189248</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
-	*[[Protein kinase C\|Protein kinase C]]	+	*[[Protein kinase C 3D structures\|Protein kinase C 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:27, 31 July 2019

OCA — Wed, 31 Jul 2019 07:27:27 GMT

←Older revision		Revision as of 07:27, 31 July 2019
Line 1:		Line 1:

	==Crystal Structure of PKCiota kinase domain==		==Crystal Structure of PKCiota kinase domain==
-	<StructureSection load='3a8w' size='340' side='right' caption='[[3a8w]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='3a8w' size='340' side='right'caption='[[3a8w]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3a8w]] is a 2 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=3A8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A8W FirstGlance]. <br>		<table><tr><td colspan='2'>[[3a8w]] is a 2 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=3A8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A8W FirstGlance]. <br>
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/3a8w_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/3a8w_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3a8w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3a8w" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Protein kinase C\|Protein kinase C]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Protein kinase C]]		[[Category: Protein kinase C]]
	[[Category: Kamata, K]]		[[Category: Kamata, K]]

OCA at 13:02, 12 October 2017

OCA — Thu, 12 Oct 2017 13:02:27 GMT

←Older revision		Revision as of 13:02, 12 October 2017
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3a8w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3a8w" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Protein kinase C\|Protein kinase C]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:53, 5 August 2016

OCA — Fri, 05 Aug 2016 10:53:47 GMT

←Older revision		Revision as of 10:53, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of PKCiota kinase domain==		==Crystal Structure of PKCiota kinase domain==
	<StructureSection load='3a8w' size='340' side='right' caption='[[3a8w]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3a8w' size='340' side='right' caption='[[3a8w]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3a8w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A8W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3a8w]] is a 2 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=3A8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A8W FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3a8v\|3a8v]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3a8v\|3a8v]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_kinase_C Protein kinase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.13 2.7.11.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_kinase_C Protein kinase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.13 2.7.11.13] </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=3a8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a8w RCSB], [http://www.ebi.ac.uk/pdbsum/3a8w PDBsum]</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=3a8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8w OCA], [http://pdbe.org/3a8w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a8w RCSB], [http://www.ebi.ac.uk/pdbsum/3a8w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a8w ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3a8w" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Protein kinase C]]		[[Category: Protein kinase C]]
	[[Category: Kamata, K]]		[[Category: Kamata, K]]

OCA at 01:45, 25 December 2014

OCA — Thu, 25 Dec 2014 01:45:43 GMT

←Older revision		Revision as of 01:45, 25 December 2014
Line 9:		Line 9:
	<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=3a8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a8w RCSB], [http://www.ebi.ac.uk/pdbsum/3a8w PDBsum]</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=3a8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a8w RCSB], [http://www.ebi.ac.uk/pdbsum/3a8w PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KPCI_HUMAN KPCI_HUMAN]] Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis.<ref>PMID:8226978</ref> <ref>PMID:9346882</ref> <ref>PMID:10467349</ref> <ref>PMID:10356400</ref> <ref>PMID:10906326</ref> <ref>PMID:11042363</ref> <ref>PMID:11724794</ref> <ref>PMID:12871960</ref> <ref>PMID:14684752</ref> <ref>PMID:15994303</ref> <ref>PMID:18270268</ref> <ref>PMID:19327373</ref> <ref>PMID:21419810</ref> <ref>PMID:21189248</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+
		+	==See Also==
		+	*[[Protein kinase C\|Protein kinase C]]
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 38:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein kinase C]]		[[Category: Protein kinase C]]
-	[[Category: Kamata, K.]]	+	[[Category: Kamata, K]]
-	[[Category: Takimura, T.]]	+	[[Category: Takimura, T]]
	[[Category: Atp complex]]		[[Category: Atp complex]]
	[[Category: Kinase domain]]		[[Category: Kinase domain]]
	[[Category: Protein kinase c iota]]		[[Category: Protein kinase c iota]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 11:59, 29 October 2014

OCA — Wed, 29 Oct 2014 11:59:12 GMT

←Older revision		Revision as of 11:59, 29 October 2014
Line 1:		Line 1:
-	[[~~Image:~~3a8w.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of PKCiota kinase domain==
		+	<StructureSection load='3a8w' size='340' side='right' caption='[[3a8w]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3a8w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A8W FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3a8v\|3a8v]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_kinase_C Protein kinase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.13 2.7.11.13] </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=3a8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a8w RCSB], [http://www.ebi.ac.uk/pdbsum/3a8w PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/3a8w_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein kinase C (PKC) plays an essential role in a wide range of cellular functions. Although crystal structures of the PKC-theta, PKC-iota and PKC-betaII kinase domains have previously been determined in complexes with small-molecule inhibitors, no structure of a PKC-substrate complex has been determined. In the previously determined PKC-iota complex, residues 533-551 in the C-terminal tail were disordered. In the present study, crystal structures of the PKC-iota kinase domain in its ATP-bound and apo forms were determined at 2.1 and 2.0 A resolution, respectively. In the ATP complex, the electron density of all of the C-terminal tail residues was well defined. In the structure, the side chain of Phe543 protrudes into the ATP-binding pocket to make van der Waals interactions with the adenine moiety of ATP; this is also observed in other AGC kinase structures such as binary and ternary substrate complexes of PKA and AKT. In addition to this interaction, the newly defined residues around the turn motif make multiple hydrogen bonds to glycine-rich-loop residues. These interactions reduce the flexibility of the glycine-rich loop, which is organized for ATP binding, and the resulting structure promotes an ATP conformation that is suitable for the subsequent phosphoryl transfer. In the case of the apo form, the structure and interaction mode of the C-terminal tail of PKC-iota are essentially identical to those of the ATP complex. These results indicate that the protein structure is pre-organized before substrate binding to PKC-iota, which is different from the case of the prototypical AGC-branch kinase PKA.

-	~~{{STRUCTURE_3a8w\| PDB=3a8w \| SCENE= }}~~	+	Structures of the PKC-iota kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533-551 in the C-terminal tail and their roles in ATP binding.,Takimura T, Kamata K, Fukasawa K, Ohsawa H, Komatani H, Yoshizumi T, Takahashi I, Kotani H, Iwasawa Y Acta Crystallogr D Biol Crystallogr. 2010 May;66(Pt 5):577-83. Epub 2010 Apr 21. PMID:20445233<ref>PMID:20445233</ref>

-	~~===Crystal Structure~~ of ~~PKCiota kinase domain===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20445233}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[3a8w]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3A8W OCA].~~	+	</StructureSection>
-		+
-	==~~See Also==~~	+
-	*[[Protein kinase C\|Protein kinase C]]	+
-		+
-	~~==Reference~~==	+
-	<~~ref group="xtra">PMID:020445233<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein kinase C]]		[[Category: Protein kinase C]]

OCA at 11:17, 20 October 2012

OCA — Sat, 20 Oct 2012 11:17:20 GMT

←Older revision		Revision as of 11:17, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3a8w]] is a 2 chain structure ~~of [[Protein kinase C]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8W OCA].	+	[[3a8w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8W OCA].

	==See Also==		==See Also==

OCA at 04:50, 26 July 2012

OCA — Thu, 26 Jul 2012 04:50:20 GMT

←Older revision		Revision as of 04:50, 26 July 2012
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	[[Image:3a8w.png\|left\|200px]]		[[Image:3a8w.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3a8w", creates the "Structure Box" on the page.
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	{{STRUCTURE_3a8w\| PDB=3a8w \| SCENE= }}		{{STRUCTURE_3a8w\| PDB=3a8w \| SCENE= }}

	===Crystal Structure of PKCiota kinase domain===		===Crystal Structure of PKCiota kinase domain===

-
-	<!--
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OCA: Protected "3a8w" [edit=sysop:move=sysop]

OCA — Wed, 04 Apr 2012 05:06:42 GMT

Protected "3a8w" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:06, 4 April 2012

OCA at 05:06, 4 April 2012

OCA — Wed, 04 Apr 2012 05:06:40 GMT

←Older revision		Revision as of 05:06, 4 April 2012
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-	~~{{Seed}}~~	+	[[Image:3a8w.png\|left\|200px]]
-	[[Image:3a8w.~~jpg~~\|left\|200px]]	+

	<!--		<!--
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	===Crystal Structure of PKCiota kinase domain===		===Crystal Structure of PKCiota kinase domain===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20445233}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20445233 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20445233}}

	==About this Structure==		==About this Structure==
-	~~3A8W~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8W OCA].	+	[[3a8w]] is a 2 chain structure of [[Protein kinase C]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8W OCA].
		+
		+	==See Also==
		+	*[[Protein kinase C\|Protein kinase C]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:020445233</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein kinase C]]		[[Category: Protein kinase C]]
Line 23:		Line 34:
	[[Category: Protein kinase c iota]]		[[Category: Protein kinase c iota]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 5 12:04:46 2010''