1tbn - Revision history

OCA at 09:11, 22 May 2024

2024-05-22T09:11:55Z

←Older revision		Revision as of 09:11, 22 May 2024
Line 20:		Line 20:
	</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=1tbn 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=1tbn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich domains of the enzyme. The natural agonist, diacylglycerol (DAG), and the natural product superagonist, phorbol dibutyrate (PDB), activate the enzyme to produce wide-ranging physiological effects. The second cysteine-rich (Cys2) domain of rat brain PKC-gamma was expressed and labeled with 15N and 13C, and the solution structure was determined to high resolution using multidimensional heteronuclear NMR methods. The phorbol binding site was identified by titrating this domain with phorbol-12,13-dibutyrate (PDB) in the presence of organic cosolvents. Titrations of this domain with lipid micelles, in the absence and presence of phorbols, indicate selective broadening of some resonances. The observed behavior indicates conformational exchange between bound and free states upon protein-micelle interaction. The data also suggest that half of the domain, including the phorbol site and one of the zinc sites, is capable of inserting into membranes.
		+
		+	NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.,Xu RX, Pawelczyk T, Xia TH, Brown SC Biochemistry. 1997 Sep 2;36(35):10709-17. PMID:9271501<ref>PMID:9271501</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1tbn" style="background-color:#fffaf0;"></div>

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

OCA at 08:39, 1 May 2024

2024-05-01T08:39:47Z

←Older revision		Revision as of 08:39, 1 May 2024
Line 1:		Line 1:

	==NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MINIMIZED AVERAGE STRUCTURE==		==NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MINIMIZED AVERAGE STRUCTURE==
-	<StructureSection load='1tbn' size='340' side='right'caption='[[1tbn~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1tbn' size='340' side='right'caption='[[1tbn]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Black_rat Black rat~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TBN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TBN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1tbo\|1tbo]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [https://pdbe.org/1tbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [https://www.ebi.ac.uk/pdbsum/1tbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tbn 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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [https://pdbe.org/1tbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [https://www.ebi.ac.uk/pdbsum/1tbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tbn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~KPCG_MOUSE KPCG_MOUSE]~~] Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also ~~contribute~~ to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage (By similarity).~~<ref>PMID~~:~~8269509</ref>~~ <ref>PMID:~~9323205~~</ref> <ref>PMID:~~11278552~~</ref> <ref>PMID:~~11356858~~</ref> <ref>PMID:~~11246146~~</ref> <ref>PMID:~~11731061~~</ref> <ref>PMID:~~17904530~~</ref>	+	[https://www.uniprot.org/uniprot/KPCG_RAT KPCG_RAT] Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity).[UniProtKB:P63318]<ref>PMID:10336135</ref> <ref>PMID:12471040</ref> <ref>PMID:15705736</ref> <ref>PMID:15936117</ref> <ref>PMID:9271501</ref> <ref>PMID:9287082</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</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=1tbn 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=1tbn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich domains of the enzyme. The natural agonist, diacylglycerol (DAG), and the natural product superagonist, phorbol dibutyrate (PDB), activate the enzyme to produce wide-ranging physiological effects. The second cysteine-rich (Cys2) domain of rat brain PKC-gamma was expressed and labeled with 15N and 13C, and the solution structure was determined to high resolution using multidimensional heteronuclear NMR methods. The phorbol binding site was identified by titrating this domain with phorbol-12,13-dibutyrate (PDB) in the presence of organic cosolvents. Titrations of this domain with lipid micelles, in the absence and presence of phorbols, indicate selective broadening of some resonances. The observed behavior indicates conformational exchange between bound and free states upon protein-micelle interaction. The data also suggest that half of the domain, including the phorbol site and one of the zinc sites, is capable of inserting into membranes.
-
-	NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.,Xu RX, Pawelczyk T, Xia TH, Brown SC Biochemistry. 1997 Sep 2;36(35):10709-17. PMID:9271501<ref>PMID:9271501</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1tbn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Black rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Brown, S C~~]]	+	[[Category: Rattus rattus]]
-	[[Category: ~~Pawelczyk, T~~]]	+	[[Category: Brown SC]]
-	[[Category: ~~Xia,~~ T]]	+	[[Category: Pawelczyk T]]
-	[[Category: ~~Xu, R X~~]]	+	[[Category: Xia T]]
-	[[Category: ~~Calcium-binding protein]]~~	+	[[Category: Xu RX]]
-	~~[[Category: Pkc]]~~	+
-	~~[[Category: Protein kinase c]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 09:25, 29 September 2021

2021-09-29T09:25:06Z

←Older revision		Revision as of 09:25, 29 September 2021
Line 3:		Line 3:
	<StructureSection load='1tbn' size='340' side='right'caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1tbn' size='340' side='right'caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Black_rat Black rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1TBN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Black_rat Black rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TBN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tbo\|1tbo]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tbo\|1tbo]]</div></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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [~~http~~://pdbe.org/1tbn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1tbn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1tbn 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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [https://pdbe.org/1tbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [https://www.ebi.ac.uk/pdbsum/1tbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tbn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/KPCG_MOUSE KPCG_MOUSE]] Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contribute to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage (By similarity).<ref>PMID:8269509</ref> <ref>PMID:9323205</ref> <ref>PMID:11278552</ref> <ref>PMID:11356858</ref> <ref>PMID:11246146</ref> <ref>PMID:11731061</ref> <ref>PMID:17904530</ref>	+	[[https://www.uniprot.org/uniprot/KPCG_MOUSE KPCG_MOUSE]] Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contribute to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage (By similarity).<ref>PMID:8269509</ref> <ref>PMID:9323205</ref> <ref>PMID:11278552</ref> <ref>PMID:11356858</ref> <ref>PMID:11246146</ref> <ref>PMID:11731061</ref> <ref>PMID:17904530</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:40, 18 December 2019

2019-12-18T13:40:51Z

←Older revision		Revision as of 13:40, 18 December 2019
Line 1:		Line 1:

	==NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MINIMIZED AVERAGE STRUCTURE==		==NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MINIMIZED AVERAGE STRUCTURE==
-	<StructureSection load='1tbn' size='340' side='right' caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1tbn' size='340' side='right'caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_rat Black rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TBN FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_rat Black rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TBN FirstGlance]. <br>
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Protein kinase C\|Protein kinase C]]	+	*[[Protein kinase C 3D structures\|Protein kinase C 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Black rat]]		[[Category: Black rat]]
		+	[[Category: Large Structures]]
	[[Category: Brown, S C]]		[[Category: Brown, S C]]
	[[Category: Pawelczyk, T]]		[[Category: Pawelczyk, T]]

OCA at 07:28, 14 March 2018

2018-03-14T07:28:04Z

←Older revision		Revision as of 07:28, 14 March 2018
Line 1:		Line 1:
		+
	==NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MINIMIZED AVERAGE STRUCTURE==		==NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MINIMIZED AVERAGE STRUCTURE==
	<StructureSection load='1tbn' size='340' side='right' caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1tbn' size='340' side='right' caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tbo\|1tbo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tbo\|1tbo]]</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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [http://pdbe.org/1tbn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [http://www.ebi.ac.uk/pdbsum/1tbn 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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [http://pdbe.org/1tbn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [http://www.ebi.ac.uk/pdbsum/1tbn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tbn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tb/1tbn_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tb/1tbn_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>

OCA at 05:49, 10 February 2016

2016-02-10T05:49:28Z

←Older revision		Revision as of 05:49, 10 February 2016
Line 17:		Line 17:
	<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=1tbn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 05:58, 11 September 2015

2015-09-11T05:58:17Z

←Older revision		Revision as of 05:58, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1tbn' size='340' side='right' caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1tbn' size='340' side='right' caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_rattus Rattus rattus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TBN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_rat Black rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TBN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tbo\|1tbo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tbo\|1tbo]]</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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [http://www.ebi.ac.uk/pdbsum/1tbn 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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [http://pdbe.org/1tbn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [http://www.ebi.ac.uk/pdbsum/1tbn PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1tbn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus rattus~~]]	+	[[Category: Black rat]]
	[[Category: Brown, S C]]		[[Category: Brown, S C]]
	[[Category: Pawelczyk, T]]		[[Category: Pawelczyk, T]]

OCA at 12:15, 25 December 2014

2014-12-25T12:15:01Z

←Older revision		Revision as of 12:15, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TBN FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TBN FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tbo\|1tbo]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tbo\|1tbo]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [http://www.ebi.ac.uk/pdbsum/1tbn 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=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [http://www.ebi.ac.uk/pdbsum/1tbn PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KPCG_MOUSE KPCG_MOUSE]] Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contribute to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage (By similarity).<ref>PMID:8269509</ref> <ref>PMID:9323205</ref> <ref>PMID:11278552</ref> <ref>PMID:11356858</ref> <ref>PMID:11246146</ref> <ref>PMID:11731061</ref> <ref>PMID:17904530</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Rattus rattus]]		[[Category: Rattus rattus]]
-	[[Category: Brown, S C.]]	+	[[Category: Brown, S C]]
-	[[Category: Pawelczyk, T.]]	+	[[Category: Pawelczyk, T]]
-	[[Category: Xia, T.]]	+	[[Category: Xia, T]]
-	[[Category: Xu, R X.]]	+	[[Category: Xu, R X]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Pkc]]		[[Category: Pkc]]
	[[Category: Protein kinase c]]		[[Category: Protein kinase c]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 20:48, 28 September 2014

2014-09-28T20:48:07Z

←Older revision		Revision as of 20:48, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1tbn.~~png~~\|~~left~~\|200px]]	+	==NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MINIMIZED AVERAGE STRUCTURE==
		+	<StructureSection load='1tbn' size='340' side='right' caption='[[1tbn]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1tbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TBN FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tbo\|1tbo]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tbn RCSB], [http://www.ebi.ac.uk/pdbsum/1tbn 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/tb/1tbn_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 ==
		+	Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich domains of the enzyme. The natural agonist, diacylglycerol (DAG), and the natural product superagonist, phorbol dibutyrate (PDB), activate the enzyme to produce wide-ranging physiological effects. The second cysteine-rich (Cys2) domain of rat brain PKC-gamma was expressed and labeled with 15N and 13C, and the solution structure was determined to high resolution using multidimensional heteronuclear NMR methods. The phorbol binding site was identified by titrating this domain with phorbol-12,13-dibutyrate (PDB) in the presence of organic cosolvents. Titrations of this domain with lipid micelles, in the absence and presence of phorbols, indicate selective broadening of some resonances. The observed behavior indicates conformational exchange between bound and free states upon protein-micelle interaction. The data also suggest that half of the domain, including the phorbol site and one of the zinc sites, is capable of inserting into membranes.

-	~~{{STRUCTURE_1tbn\| PDB=1tbn \| SCENE= }}~~	+	NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.,Xu RX, Pawelczyk T, Xia TH, Brown SC Biochemistry. 1997 Sep 2;36(35):10709-17. PMID:9271501<ref>PMID:9271501</ref>

-	~~===NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN~~, ~~MINIMIZED AVERAGE STRUCTURE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9271501}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1tbn]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_rattus Rattus rattus]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA].~~	+

	==See Also==		==See Also==
	*[[Protein kinase C\|Protein kinase C]]		*[[Protein kinase C\|Protein kinase C]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009271501<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Rattus rattus]]		[[Category: Rattus rattus]]
	[[Category: Brown, S C.]]		[[Category: Brown, S C.]]

OCA at 16:32, 20 October 2012

2012-10-20T16:32:49Z

←Older revision		Revision as of 16:32, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1tbn]] is a 1 chain structure ~~of [[Protein kinase C]]~~ with sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA].	+	[[1tbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBN OCA].

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