3aqv - Revision history

OCA at 14:32, 1 November 2023

OCA — Wed, 01 Nov 2023 14:32:53 GMT

←Older revision		Revision as of 14:32, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3aqv' size='340' side='right'caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>		<StructureSection load='3aqv' size='340' side='right'caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aqv]] is a 1 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=3AQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AQV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aqv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AQV FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=TAK:6~~-[~~4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO~~[~~1,5-A~~]~~PYRIMIDINE'>TAK</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]] 2.08Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[2yza\|2yza]], [[2h6d\|2h6d]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Non~~-~~specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number~~ [~~https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=~~2~~.7.11.~~1 ~~2.7.11.~~1] </~~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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [https://pdbe.org/3aqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [https://www.ebi.ac.uk/pdbsum/3aqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqv 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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [https://pdbe.org/3aqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [https://www.ebi.ac.uk/pdbsum/3aqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[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 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Handa N]]
-	[[Category: Handa, N]]	+	[[Category: Kishishita S]]
-	[[Category: Kishishita, S]]	+	[[Category: Saijo S]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Shirouzu M]]
-	[[Category: Saijo, S]]	+	[[Category: Takagi T]]
-	[[Category: Shirouzu, M]]	+	[[Category: Terada T]]
-	[[Category: Takagi, T]]	+	[[Category: Toyama M]]
-	[[Category: Terada, T]]	+	[[Category: Yokoyama S]]
-	[[Category: Toyama, M]]	+
-	[[Category: Yokoyama, S]]	+
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: Cholesterol biosynthesis]]~~	+
-	~~[[Category: Fatty acid biosynthesis]]~~	+
-	~~[[Category: Glucose metabolism]]~~	+
-	~~[[Category: Lipid synthesis]]~~	+
-	~~[[Category: Magnesium]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Rsgi]]~~	+
-	~~[[Category: Serine/threonine protein kinase]]~~	+
-	~~[[Category: Serine/threonine-protein kinase]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Steroid biosynthesis]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 13:26, 4 May 2022

OCA — Wed, 04 May 2022 13:26:55 GMT

←Older revision		Revision as of 13:26, 4 May 2022
Line 3:		Line 3:
	<StructureSection load='3aqv' size='340' side='right'caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>		<StructureSection load='3aqv' size='340' side='right'caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aqv]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3AQV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aqv]] is a 1 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=3AQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AQV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yza\|2yza]], [[2h6d\|2h6d]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2yza\|2yza]], [[2h6d\|2h6d]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [~~http~~://pdbe.org/3aqv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3aqv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqv 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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [https://pdbe.org/3aqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [https://www.ebi.ac.uk/pdbsum/3aqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqv 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>	+	[[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 ==

OCA at 12:24, 29 July 2020

OCA — Wed, 29 Jul 2020 12:24:41 GMT

←Older revision		Revision as of 12:24, 29 July 2020
Line 1:		Line 1:

	==Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C==		==Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C==
-	<StructureSection load='3aqv' size='340' side='right' caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>	+	<StructureSection load='3aqv' size='340' side='right'caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aqv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQV OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3AQV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aqv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3AQV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yza\|2yza]], [[2h6d\|2h6d]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yza\|2yza]], [[2h6d\|2h6d]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [http://pdbe.org/3aqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [http://www.ebi.ac.uk/pdbsum/3aqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqv ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [http://pdbe.org/3aqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [http://www.ebi.ac.uk/pdbsum/3aqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[AMP-activated protein kinase\|AMP-activated protein kinase]]	+	*[[AMP-activated protein kinase 3D structures\|AMP-activated protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Handa, N]]		[[Category: Handa, N]]

OCA at 19:48, 11 August 2016

OCA — Thu, 11 Aug 2016 19:48:47 GMT

←Older revision		Revision as of 19:48, 11 August 2016
Line 1:		Line 1:
		+
	==Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C==		==Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C==
	<StructureSection load='3aqv' size='340' side='right' caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>		<StructureSection load='3aqv' size='340' side='right' caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aqv]] is a 1 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=3AQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AQV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aqv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AQV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yza\|2yza]], [[2h6d\|2h6d]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yza\|2yza]], [[2h6d\|2h6d]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [http://www.ebi.ac.uk/pdbsum/3aqv 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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [http://pdbe.org/3aqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [http://www.ebi.ac.uk/pdbsum/3aqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 3aqv" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Handa, N]]		[[Category: Handa, N]]

OCA at 10:21, 25 January 2015

OCA — Sun, 25 Jan 2015 10:21:10 GMT

←Older revision		Revision as of 10:21, 25 January 2015
Line 8:		Line 8:
	<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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [http://www.ebi.ac.uk/pdbsum/3aqv 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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [http://www.ebi.ac.uk/pdbsum/3aqv PDBsum]</span></td></tr>
	</table>		</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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 27:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Handa, N.]]	+	[[Category: Handa, N]]
-	[[Category: Kishishita, S.]]	+	[[Category: Kishishita, S]]
-	[[Category: ~~RSGI, RIKEN~~ Structural ~~Genomics/Proteomics Initiative.~~]]	+	[[Category: Structural genomic]]
-	[[Category: Saijo, S.]]	+	[[Category: Saijo, S]]
-	[[Category: Shirouzu, M.]]	+	[[Category: Shirouzu, M]]
-	[[Category: Takagi, T.]]	+	[[Category: Takagi, T]]
-	[[Category: Terada, T.]]	+	[[Category: Terada, T]]
-	[[Category: Toyama, M.]]	+	[[Category: Toyama, M]]
-	[[Category: Yokoyama, S.]]	+	[[Category: Yokoyama, S]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Cholesterol biosynthesis]]		[[Category: Cholesterol biosynthesis]]
Line 43:		Line 45:
	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]
	[[Category: Phosphorylation]]		[[Category: Phosphorylation]]
-	[[Category: Riken structural genomics/proteomics initiative]]
	[[Category: Rsgi]]		[[Category: Rsgi]]
	[[Category: Serine/threonine protein kinase]]		[[Category: Serine/threonine protein kinase]]
Line 49:		Line 50:
	[[Category: Signaling protein]]		[[Category: Signaling protein]]
	[[Category: Steroid biosynthesis]]		[[Category: Steroid biosynthesis]]
-	[[Category: Structural genomic]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 09:28, 5 November 2014

OCA — Wed, 05 Nov 2014 09:28:27 GMT

←Older revision		Revision as of 09:28, 5 November 2014
Line 1:		Line 1:
-	[[~~Image:~~3aqv.~~png~~\|~~left~~\|~~200px~~]]	+	==Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C==
		+	<StructureSection load='3aqv' size='340' side='right' caption='[[3aqv]], [[Resolution\|resolution]] 2.08Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3aqv]] is a 1 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=3AQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AQV FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yza\|2yza]], [[2h6d\|2h6d]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aqv RCSB], [http://www.ebi.ac.uk/pdbsum/3aqv PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	AMP-activated protein kinase (AMPK) is a serine/threonine kinase that functions as a sensor to maintain energy balance at both the cellular and the whole-body levels and is therefore a potential target for drug design against metabolic syndrome, obesity and type 2 diabetes. Here, the crystal structure of the phosphorylated-state mimic T172D mutant kinase domain from the human AMPK alpha2 subunit is reported in the apo form and in complex with a selective inhibitor, compound C. The AMPK alpha2 kinase domain exhibits a typical bilobal kinase fold and exists as a monomer in the crystal. Like the wild-type apo form, the T172D mutant apo form adopts the autoinhibited structure of the `DFG-out' conformation, with the Phe residue of the DFG motif anchored within the putative ATP-binding pocket. Compound C binding dramatically alters the conformation of the activation loop, which adopts an intermediate conformation between DFG-out and DFG-in. This induced fit forms a compound-C binding pocket composed of the N-lobe, the C-lobe and the hinge of the kinase domain. The pocket partially overlaps with the putative ATP-binding pocket. These three-dimensional structures will be useful to guide drug discovery.

-	~~{{STRUCTURE_3aqv\| PDB=3aqv \| SCENE= }}~~	+	Structural basis for compound C inhibition of the human AMP-activated protein kinase alpha2 subunit kinase domain.,Handa N, Takagi T, Saijo S, Kishishita S, Takaya D, Toyama M, Terada T, Shirouzu M, Suzuki A, Lee S, Yamauchi T, Okada-Iwabu M, Iwabu M, Kadowaki T, Minokoshi Y, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):480-7. Epub 2011 Apr 14. PMID:21543851<ref>PMID:21543851</ref>

-	~~===Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21543851}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3aqv]] is~~ a ~~1 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=3AQV OCA].~~	+

	==See Also==		==See Also==
	*[[AMP-activated protein kinase\|AMP-activated protein kinase]]		*[[AMP-activated protein kinase\|AMP-activated protein kinase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:021543851<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]

OCA at 13:24, 20 October 2012

OCA — Sat, 20 Oct 2012 13:24:32 GMT

←Older revision		Revision as of 13:24, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3aqv]] is a 1 chain structure ~~of [[AMP-activated protein kinase]]~~ 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=3AQV OCA].	+	[[3aqv]] is a 1 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=3AQV OCA].

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

OCA at 11:51, 26 July 2012

OCA — Thu, 26 Jul 2012 11:51:44 GMT

←Older revision		Revision as of 11:51, 26 July 2012
Line 1:		Line 1:
	[[Image:3aqv.png\|left\|200px]]		[[Image:3aqv.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3aqv", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3aqv\| PDB=3aqv \| SCENE= }}		{{STRUCTURE_3aqv\| PDB=3aqv \| SCENE= }}

	===Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C===		===Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21543851}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21543851 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_21543851}}		{{ABSTRACT_PUBMED_21543851}}

	==About this Structure==		==About this Structure==
-	[[3aqv]] is a 1 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=3AQV OCA].	+	[[3aqv]] is a 1 chain structure of [[AMP-activated protein kinase]] 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=3AQV OCA].
		+
		+	==See Also==
		+	*[[AMP-activated protein kinase\|AMP-activated protein kinase]]

	==Reference==		==Reference==

OCA at 06:04, 11 April 2012

OCA — Wed, 11 Apr 2012 06:04:05 GMT

←Older revision		Revision as of 06:04, 11 April 2012
Line 1:		Line 1:
-	[[Image:3aqv.~~jpg~~\|left\|200px]]	+	[[Image:3aqv.png\|left\|200px]]

	<!--		<!--
Line 11:		Line 11:
	===Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C===		===Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21543851}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21543851 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21543851}}

	==About this Structure==		==About this Structure==
	[[3aqv]] is a 1 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=3AQV OCA].		[[3aqv]] is a 1 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=3AQV OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021543851</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
Line 25:		Line 34:
	[[Category: Toyama, M.]]		[[Category: Toyama, M.]]
	[[Category: Yokoyama, S.]]		[[Category: Yokoyama, S.]]
		+	[[Category: Atp-binding]]
		+	[[Category: Cholesterol biosynthesis]]
		+	[[Category: Fatty acid biosynthesis]]
		+	[[Category: Glucose metabolism]]
		+	[[Category: Lipid synthesis]]
		+	[[Category: Magnesium]]
		+	[[Category: Metal-binding]]
		+	[[Category: Nucleotide-binding]]
		+	[[Category: Phosphorylation]]
		+	[[Category: Riken structural genomics/proteomics initiative]]
		+	[[Category: Rsgi]]
		+	[[Category: Serine/threonine protein kinase]]
		+	[[Category: Serine/threonine-protein kinase]]
		+	[[Category: Signaling protein]]
		+	[[Category: Steroid biosynthesis]]
		+	[[Category: Structural genomic]]
		+	[[Category: Transferase]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 07:22, 27 April 2011

OCA — Wed, 27 Apr 2011 07:22:23 GMT

←Older revision		Revision as of 07:22, 27 April 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3aqv.jpg\|left\|200px]]

-	The ~~entry 3aqv~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3aqv", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3aqv\| PDB=3aqv \| SCENE= }}

-	~~Authors: Handa, N., Takagi, T., Saijo, S., Kishishita, S., Toyama, M., Terada, T., Shirouzu, M., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative~~ (~~RSGI~~)	+	===Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C===

-	~~Description~~:	+
		+	==About this Structure==
		+	[[3aqv]] is a 1 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=3AQV OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Handa, N.]]
		+	[[Category: Kishishita, S.]]
		+	[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
		+	[[Category: Saijo, S.]]
		+	[[Category: Shirouzu, M.]]
		+	[[Category: Takagi, T.]]
		+	[[Category: Terada, T.]]
		+	[[Category: Toyama, M.]]
		+	[[Category: Yokoyama, S.]]