4zhx - Revision history

OCA at 08:18, 27 September 2023

OCA — Wed, 27 Sep 2023 08:18:14 GMT

←Older revision		Revision as of 08:18, 27 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4zhx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZHX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4zhx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZHX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4O7:(5S,6R,7R,9R,13CR,14R,16AS)-6-METHOXY-5-METHYL-7-(METHYLAMINO)-6,7,8,9,14,15,16,16A-OCTAHYDRO-5H,13CH-5,9-EPOXY-4B,9A,15-TRIAZADIBENZO[B,H]CYCLONONA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-14-OL'>4O7</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=C1V:3-[4-(2-HYDROXYPHENYL)PHENYL]-4-OXIDANYL-6-OXIDANYLIDENE-7H-THIENO[2,3-B]PYRIDINE-5-CARBONITRILE'>C1V</scene>, <scene name='pdbligand=C2Z:5-(5-HYDROXYL-ISOXAZOL-3-YL)-FURAN-2-PHOSPHONIC+ACID'>C2Z</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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]] 2.99Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4O7:(5S,6R,7R,9R,13CR,14R,16AS)-6-METHOXY-5-METHYL-7-(METHYLAMINO)-6,7,8,9,14,15,16,16A-OCTAHYDRO-5H,13CH-5,9-EPOXY-4B,9A,15-TRIAZADIBENZO[B,H]CYCLONONA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-14-OL'>4O7</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=C1V:3-[4-(2-HYDROXYPHENYL)PHENYL]-4-OXIDANYL-6-OXIDANYLIDENE-7H-THIENO[2,3-B]PYRIDINE-5-CARBONITRILE'>C1V</scene>, <scene name='pdbligand=C2Z:5-(5-HYDROXYL-ISOXAZOL-3-YL)-FURAN-2-PHOSPHONIC+ACID'>C2Z</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zhx OCA], [https://pdbe.org/4zhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zhx RCSB], [https://www.ebi.ac.uk/pdbsum/4zhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zhx 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=4zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zhx OCA], [https://pdbe.org/4zhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zhx RCSB], [https://www.ebi.ac.uk/pdbsum/4zhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zhx ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:28, 18 May 2023

OCA — Thu, 18 May 2023 07:28:31 GMT

←Older revision		Revision as of 07:28, 18 May 2023
Line 3:		Line 3:
	<StructureSection load='4zhx' size='340' side='right'caption='[[4zhx]], [[Resolution\|resolution]] 2.99Å' scene=''>		<StructureSection load='4zhx' size='340' side='right'caption='[[4zhx]], [[Resolution\|resolution]] 2.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4zhx]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZHX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4ZHX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4zhx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZHX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4O7:(5S,6R,7R,9R,13CR,14R,16AS)-6-METHOXY-5-METHYL-7-(METHYLAMINO)-6,7,8,9,14,15,16,16A-OCTAHYDRO-5H,13CH-5,9-EPOXY-4B,9A,15-TRIAZADIBENZO[B,H]CYCLONONA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-14-OL'>4O7</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=C1V:3-[4-(2-HYDROXYPHENYL)PHENYL]-4-OXIDANYL-6-OXIDANYLIDENE-7H-THIENO[2,3-B]PYRIDINE-5-CARBONITRILE'>C1V</scene>, <scene name='pdbligand=C2Z:5-(5-HYDROXYL-ISOXAZOL-3-YL)-FURAN-2-PHOSPHONIC+ACID'>C2Z</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4O7:(5S,6R,7R,9R,13CR,14R,16AS)-6-METHOXY-5-METHYL-7-(METHYLAMINO)-6,7,8,9,14,15,16,16A-OCTAHYDRO-5H,13CH-5,9-EPOXY-4B,9A,15-TRIAZADIBENZO[B,H]CYCLONONA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-14-OL'>4O7</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=C1V:3-[4-(2-HYDROXYPHENYL)PHENYL]-4-OXIDANYL-6-OXIDANYLIDENE-7H-THIENO[2,3-B]PYRIDINE-5-CARBONITRILE'>C1V</scene>, <scene name='pdbligand=C2Z:5-(5-HYDROXYL-ISOXAZOL-3-YL)-FURAN-2-PHOSPHONIC+ACID'>C2Z</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <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=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zhx OCA], [https://pdbe.org/4zhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zhx RCSB], [https://www.ebi.ac.uk/pdbsum/4zhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zhx 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=4zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zhx OCA], [~~http~~://pdbe.org/4zhx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4zhx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4zhx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4zhx ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AAPK2_HUMAN AAPK2_HUMAN]] Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.<ref>PMID:7959015</ref> <ref>PMID:11554766</ref> <ref>PMID:11518699</ref> <ref>PMID:12519745</ref> <ref>PMID:14651849</ref> <ref>PMID:15866171</ref> <ref>PMID:17711846</ref> <ref>PMID:17486097</ref> <ref>PMID:18184930</ref> <ref>PMID:20074060</ref> <ref>PMID:20160076</ref> <ref>PMID:21205641</ref> [[http://www.uniprot.org/uniprot/AAKG1_HUMAN AAKG1_HUMAN]] AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:21680840</ref> [[http://www.uniprot.org/uniprot/AAKB1_HUMAN AAKB1_HUMAN]] Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).	+	[https://www.uniprot.org/uniprot/AAPK2_HUMAN AAPK2_HUMAN] Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.<ref>PMID:7959015</ref> <ref>PMID:11554766</ref> <ref>PMID:11518699</ref> <ref>PMID:12519745</ref> <ref>PMID:14651849</ref> <ref>PMID:15866171</ref> <ref>PMID:17711846</ref> <ref>PMID:17486097</ref> <ref>PMID:18184930</ref> <ref>PMID:20074060</ref> <ref>PMID:20160076</ref> <ref>PMID:21205641</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Gorman~~, M A~~]]	+	[[Category: Gorman MA]]
-	[[Category: Issa~~, S M.A~~]]	+	[[Category: Issa SMA]]
-	[[Category: Kemp~~, B E~~]]	+	[[Category: Kemp BE]]
-	[[Category: Langendorf~~, C G~~]]	+	[[Category: Langendorf CG]]
-	[[Category: Ling, N]]	+	[[Category: Ling N]]
-	[[Category: Ngoei~~, K R~~]]	+	[[Category: Ngoei KR]]
-	[[Category: Oakhill~~, J S~~]]	+	[[Category: Oakhill JS]]
-	[[Category: Parker~~, M W~~]]	+	[[Category: Parker MW]]
-	[[Category: Sakamoto, K]]	+	[[Category: Sakamoto K]]
-	[[Category: Scott~~, J W]]~~	+	[[Category: Scott JW]]
-	~~[[Category: Allosteric activation]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Serine/threonine kinase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:50, 4 March 2020

OCA — Wed, 04 Mar 2020 07:50:54 GMT

←Older revision		Revision as of 07:50, 4 March 2020
Line 1:		Line 1:

	==Novel binding site for allosteric activation of AMPK==		==Novel binding site for allosteric activation of AMPK==
-	<StructureSection load='4zhx' size='340' side='right' caption='[[4zhx]], [[Resolution\|resolution]] 2.99Å' scene=''>	+	<StructureSection load='4zhx' size='340' side='right'caption='[[4zhx]], [[Resolution\|resolution]] 2.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4zhx]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZHX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4zhx]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZHX FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4zhx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4zhx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[AMP-activated protein kinase 3D structures\|AMP-activated protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Gorman, M A]]		[[Category: Gorman, M A]]
	[[Category: Issa, S M.A]]		[[Category: Issa, S M.A]]

OCA at 12:21, 6 November 2017

OCA — Mon, 06 Nov 2017 12:21:06 GMT

←Older revision		Revision as of 12:21, 6 November 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4zhx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4zhx" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[AMP-activated protein kinase\|AMP-activated protein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:38, 27 September 2017

OCA — Wed, 27 Sep 2017 09:38:41 GMT

←Older revision		Revision as of 09:38, 27 September 2017
Line 6:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4O7:(5S,6R,7R,9R,13CR,14R,16AS)-6-METHOXY-5-METHYL-7-(METHYLAMINO)-6,7,8,9,14,15,16,16A-OCTAHYDRO-5H,13CH-5,9-EPOXY-4B,9A,15-TRIAZADIBENZO[B,H]CYCLONONA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-14-OL'>4O7</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=C1V:3-[4-(2-HYDROXYPHENYL)PHENYL]-4-OXIDANYL-6-OXIDANYLIDENE-7H-THIENO[2,3-B]PYRIDINE-5-CARBONITRILE'>C1V</scene>, <scene name='pdbligand=C2Z:5-(5-HYDROXYL-ISOXAZOL-3-YL)-FURAN-2-PHOSPHONIC+ACID'>C2Z</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4O7:(5S,6R,7R,9R,13CR,14R,16AS)-6-METHOXY-5-METHYL-7-(METHYLAMINO)-6,7,8,9,14,15,16,16A-OCTAHYDRO-5H,13CH-5,9-EPOXY-4B,9A,15-TRIAZADIBENZO[B,H]CYCLONONA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-14-OL'>4O7</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=C1V:3-[4-(2-HYDROXYPHENYL)PHENYL]-4-OXIDANYL-6-OXIDANYLIDENE-7H-THIENO[2,3-B]PYRIDINE-5-CARBONITRILE'>C1V</scene>, <scene name='pdbligand=C2Z:5-(5-HYDROXYL-ISOXAZOL-3-YL)-FURAN-2-PHOSPHONIC+ACID'>C2Z</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <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=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></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=4zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zhx OCA], [http://pdbe.org/4zhx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zhx RCSB], [http://www.ebi.ac.uk/pdbsum/4zhx 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=4zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zhx OCA], [http://pdbe.org/4zhx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zhx RCSB], [http://www.ebi.ac.uk/pdbsum/4zhx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zhx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4zhx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4zhx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[AMP-activated protein kinase\|AMP-activated protein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:00, 10 May 2016

OCA — Tue, 10 May 2016 17:00:16 GMT

←Older revision		Revision as of 17:00, 10 May 2016
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/AAPK2_HUMAN AAPK2_HUMAN]] Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.<ref>PMID:7959015</ref> <ref>PMID:11554766</ref> <ref>PMID:11518699</ref> <ref>PMID:12519745</ref> <ref>PMID:14651849</ref> <ref>PMID:15866171</ref> <ref>PMID:17711846</ref> <ref>PMID:17486097</ref> <ref>PMID:18184930</ref> <ref>PMID:20074060</ref> <ref>PMID:20160076</ref> <ref>PMID:21205641</ref> [[http://www.uniprot.org/uniprot/AAKG1_HUMAN AAKG1_HUMAN]] AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:21680840</ref> [[http://www.uniprot.org/uniprot/AAKB1_HUMAN AAKB1_HUMAN]] Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).		[[http://www.uniprot.org/uniprot/AAPK2_HUMAN AAPK2_HUMAN]] Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.<ref>PMID:7959015</ref> <ref>PMID:11554766</ref> <ref>PMID:11518699</ref> <ref>PMID:12519745</ref> <ref>PMID:14651849</ref> <ref>PMID:15866171</ref> <ref>PMID:17711846</ref> <ref>PMID:17486097</ref> <ref>PMID:18184930</ref> <ref>PMID:20074060</ref> <ref>PMID:20160076</ref> <ref>PMID:21205641</ref> [[http://www.uniprot.org/uniprot/AAKG1_HUMAN AAKG1_HUMAN]] AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:21680840</ref> [[http://www.uniprot.org/uniprot/AAKB1_HUMAN AAKB1_HUMAN]] Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The metabolic stress-sensing enzyme AMP-activated protein kinase (AMPK) is responsible for regulating metabolism in response to energy supply and demand. Drugs that activate AMPK may be useful in the treatment of metabolic diseases including type 2 diabetes. We have determined the crystal structure of AMPK in complex with its activator 5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid (C2), revealing two C2-binding sites in the gamma-subunit distinct from nucleotide sites. C2 acts synergistically with the drug A769662 to activate AMPK alpha1-containing complexes independent of upstream kinases. Our results show that dual drug therapies could be effective AMPK-targeting strategies to treat metabolic diseases.
		+
		+	Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding.,Langendorf CG, Ngoei KR, Scott JW, Ling NX, Issa SM, Gorman MA, Parker MW, Sakamoto K, Oakhill JS, Kemp BE Nat Commun. 2016 Mar 8;7:10912. doi: 10.1038/ncomms10912. PMID:26952388<ref>PMID:26952388</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4zhx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:51, 10 March 2016

OCA — Thu, 10 Mar 2016 03:51:22 GMT

←Older revision		Revision as of 03:51, 10 March 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 4zhx is ~~ON HOLD until Paper Publication~~	+	==Novel binding site for allosteric activation of AMPK==
-		+	<StructureSection load='4zhx' size='340' side='right' caption='[[4zhx]], [[Resolution\|resolution]] 2.99Å' scene=''>
-	~~Authors~~: ~~Langendorf~~, C.G., ~~Ngoei~~, K.R., ~~Issa~~, S.M.A., ~~Ling~~, N., ~~Gorman~~, M.A., ~~Parker~~, M.W., ~~Sakamoto~~, K., ~~Scott~~, J.W., ~~Oakhill~~, J.S., Kemp, B.E.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4zhx]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZHX FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4O7:(5S,6R,7R,9R,13CR,14R,16AS)-6-METHOXY-5-METHYL-7-(METHYLAMINO)-6,7,8,9,14,15,16,16A-OCTAHYDRO-5H,13CH-5,9-EPOXY-4B,9A,15-TRIAZADIBENZO[B,H]CYCLONONA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-14-OL'>4O7</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=C1V:3-[4-(2-HYDROXYPHENYL)PHENYL]-4-OXIDANYL-6-OXIDANYLIDENE-7H-THIENO[2,3-B]PYRIDINE-5-CARBONITRILE'>C1V</scene>, <scene name='pdbligand=C2Z:5-(5-HYDROXYL-ISOXAZOL-3-YL)-FURAN-2-PHOSPHONIC+ACID'>C2Z</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=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></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=4zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zhx OCA], [http://pdbe.org/4zhx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zhx RCSB], [http://www.ebi.ac.uk/pdbsum/4zhx PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AAPK2_HUMAN AAPK2_HUMAN]] Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.<ref>PMID:7959015</ref> <ref>PMID:11554766</ref> <ref>PMID:11518699</ref> <ref>PMID:12519745</ref> <ref>PMID:14651849</ref> <ref>PMID:15866171</ref> <ref>PMID:17711846</ref> <ref>PMID:17486097</ref> <ref>PMID:18184930</ref> <ref>PMID:20074060</ref> <ref>PMID:20160076</ref> <ref>PMID:21205641</ref> [[http://www.uniprot.org/uniprot/AAKG1_HUMAN AAKG1_HUMAN]] AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:21680840</ref> [[http://www.uniprot.org/uniprot/AAKB1_HUMAN AAKB1_HUMAN]] Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Gorman, M A]]
		+	[[Category: Issa, S M.A]]
		+	[[Category: Kemp, B E]]
		+	[[Category: Langendorf, C G]]
		+	[[Category: Ling, N]]
		+	[[Category: Ngoei, K R]]
		+	[[Category: Oakhill, J S]]
		+	[[Category: Parker, M W]]
	[[Category: Sakamoto, K]]		[[Category: Sakamoto, K]]
-	~~[[Category: Gorman, M.A]]~~	+	[[Category: Scott, J W]]
-	~~[[Category: Parker, M.W]]~~	+	[[Category: Allosteric activation]]
-	[[Category: Scott, J.W]]	+	[[Category: Nucleotide-binding]]
-	[[Category: ~~Oakhill, J.S~~]]	+	[[Category: Serine/threonine kinase]]
-	[[Category: ~~Ngoei, K.R~~]]	+	[[Category: Transferase]]
-	[[Category: ~~Kemp, B.E~~]]	+
-	[[Category: ~~Issa, S.M.A]]~~	+
-	~~[[Category: Langendorf, C.G]]~~	+
-	~~[[Category: Ling, N~~]]	+

OCA at 00:02, 1 December 2015

OCA — Tue, 01 Dec 2015 00:02:02 GMT

←Older revision		Revision as of 00:02, 1 December 2015
Line 7:		Line 7:
	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Parker, M.W]]
-	[[Category: Scott, J.W]]
-	[[Category: Ngoei, K.R]]
-	[[Category: Issa, S.M.A]]
-	[[Category: Ling, N]]
	[[Category: Sakamoto, K]]		[[Category: Sakamoto, K]]
	[[Category: Gorman, M.A]]		[[Category: Gorman, M.A]]
		+	[[Category: Parker, M.W]]
		+	[[Category: Scott, J.W]]
	[[Category: Oakhill, J.S]]		[[Category: Oakhill, J.S]]
		+	[[Category: Ngoei, K.R]]
	[[Category: Kemp, B.E]]		[[Category: Kemp, B.E]]
		+	[[Category: Issa, S.M.A]]
	[[Category: Langendorf, C.G]]		[[Category: Langendorf, C.G]]
		+	[[Category: Ling, N]]

OCA at 10:53, 3 June 2015

OCA — Wed, 03 Jun 2015 10:53:36 GMT

←Older revision		Revision as of 10:53, 3 June 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4zhx is ON HOLD	+	The entry 4zhx is ON HOLD until Paper Publication

	Authors: Langendorf, C.G., Ngoei, K.R., Issa, S.M.A., Ling, N., Gorman, M.A., Parker, M.W., Sakamoto, K., Scott, J.W., Oakhill, J.S., Kemp, B.E.		Authors: Langendorf, C.G., Ngoei, K.R., Issa, S.M.A., Ling, N., Gorman, M.A., Parker, M.W., Sakamoto, K., Scott, J.W., Oakhill, J.S., Kemp, B.E.

OCA: Protected "4zhx" [edit=sysop:move=sysop]

OCA — Wed, 06 May 2015 11:44:52 GMT

Protected "4zhx" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:44, 6 May 2015