6eru - Revision history

OCA at 08:12, 21 May 2019

2019-05-21T08:12:06Z

←Older revision		Revision as of 08:12, 21 May 2019
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	==Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in complex with compound RKp120==		==Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in complex with compound RKp120==
-	<StructureSection load='6eru' size='340' side='right' caption='[[6eru]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='6eru' size='340' side='right'caption='[[6eru]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6eru]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ERU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ERU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6eru]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cho_cell_lines Cho cell lines]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ERU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ERU FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BWB:'>BWB</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BWB:'>BWB</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRKACA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10029 CHO cell lines])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] </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=6eru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eru OCA], [http://pdbe.org/6eru PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eru RCSB], [http://www.ebi.ac.uk/pdbsum/6eru PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eru 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=6eru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eru OCA], [http://pdbe.org/6eru PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eru RCSB], [http://www.ebi.ac.uk/pdbsum/6eru PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eru ProSAT]</span></td></tr>
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	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KAPCA_CRIGR KAPCA_CRIGR]] Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (By similarity).		[[http://www.uniprot.org/uniprot/KAPCA_CRIGR KAPCA_CRIGR]] Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (By similarity).
		+
		+	==See Also==
		+	*[[CAMP-dependent protein kinase 3D structures\|CAMP-dependent protein kinase 3D structures]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Cho cell lines]]
		+	[[Category: Large Structures]]
	[[Category: CAMP-dependent protein kinase]]		[[Category: CAMP-dependent protein kinase]]
	[[Category: Heine, A]]		[[Category: Heine, A]]

OCA at 06:54, 31 October 2018

2018-10-31T06:54:19Z

←Older revision		Revision as of 06:54, 31 October 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6eru is ~~ON HOLD until Paper Publication~~	+	==Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in complex with compound RKp120==
-		+	<StructureSection load='6eru' size='340' side='right' caption='[[6eru]], [[Resolution\|resolution]] 2.15Å' scene=''>
-	~~Authors~~: ~~Mueller~~, J.M., ~~Heine~~, A., ~~Klebe~~, G.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6eru]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ERU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ERU FirstGlance]. <br>
-	~~Description~~: ~~Crystal Structure~~ of the ~~Protein~~-~~Kinase A catalytic subunit~~ from ~~Criteculus Griseus~~ in complex with ~~compound RKp120~~	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BWB:'>BWB</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] </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=6eru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eru OCA], [http://pdbe.org/6eru PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eru RCSB], [http://www.ebi.ac.uk/pdbsum/6eru PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eru ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KAPCA_CRIGR KAPCA_CRIGR]] Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (By similarity).
		+	__TOC__
		+	</StructureSection>
		+	[[Category: CAMP-dependent protein kinase]]
	[[Category: Heine, A]]		[[Category: Heine, A]]
-	[[Category: Mueller, J.M]]
	[[Category: Klebe, G]]		[[Category: Klebe, G]]
		+	[[Category: Mueller, J M]]
		+	[[Category: Complex]]
		+	[[Category: Peptidic ligand]]
		+	[[Category: Transferase]]

OCA at 06:27, 15 November 2017

2017-11-15T06:27:25Z

←Older revision		Revision as of 06:27, 15 November 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6eru is ON HOLD	+	The entry 6eru is ON HOLD until Paper Publication

	Authors: Mueller, J.M., Heine, A., Klebe, G.		Authors: Mueller, J.M., Heine, A., Klebe, G.

OCA at 05:04, 1 November 2017

2017-11-01T05:04:13Z

←Older revision		Revision as of 05:04, 1 November 2017
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6eru is ON HOLD ~~until sometime in the future~~	+	The entry 6eru is ON HOLD

	Authors: Mueller, J.M., Heine, A., Klebe, G.		Authors: Mueller, J.M., Heine, A., Klebe, G.

OCA: Protected "6eru" [edit=sysop:move=sysop]

2017-10-25T06:03:29Z

Protected "6eru" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:03, 25 October 2017

OCA: New page: '''Unreleased structure''' The entry 6eru is ON HOLD until sometime in the future Authors: Mueller, J.M., Heine, A., Klebe, G. Description: Crystal Structure of the Protein-Kinase A ca...

2017-10-25T06:03:28Z

New page: '''Unreleased structure''' The entry 6eru is ON HOLD until sometime in the future Authors: Mueller, J.M., Heine, A., Klebe, G. Description: Crystal Structure of the Protein-Kinase A ca...

New page

'''Unreleased structure'''

The entry 6eru is ON HOLD until sometime in the future

Authors: Mueller, J.M., Heine, A., Klebe, G.

Description: Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in complex with compound RKp120
[[Category: Unreleased Structures]]
[[Category: Heine, A]]
[[Category: Mueller, J.M]]
[[Category: Klebe, G]]