5lcr - Revision history

OCA at 08:56, 11 October 2023

OCA — Wed, 11 Oct 2023 08:56:23 GMT

←Older revision		Revision as of 08:56, 11 October 2023
Line 3:		Line 3:
	<StructureSection load='5lcr' size='340' side='right'caption='[[5lcr]], [[Resolution\|resolution]] 1.56Å' scene=''>		<StructureSection load='5lcr' size='340' side='right'caption='[[5lcr]], [[Resolution\|resolution]] 1.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lcr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5LCR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lcr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LCR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6TX:2-[isoquinolin-5-ylsulfonyl(propyl)amino]ethylazanium'>6TX</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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]] 1.565Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6TX:2-[isoquinolin-5-ylsulfonyl(propyl)amino]ethylazanium'>6TX</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5lcp\|5lcp]], [[5lcq\|5lcq]]</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=5lcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcr OCA], [https://pdbe.org/5lcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lcr RCSB], [https://www.ebi.ac.uk/pdbsum/5lcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcr ProSAT]</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~~://proteopedia.org/fgij/fg.htm?mol=5lcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcr OCA], [~~http~~://pdbe.org/5lcr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5lcr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5lcr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcr ProSAT]</span></td></tr>	+
	</table>		</table>
	== 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/IPKA_HUMAN IPKA_HUMAN]] Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.	+	[https://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==		==See Also==
Line 17:		Line 15:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Cricetulus griseus]]
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: CAMP-dependent protein kinase]]~~	+	[[Category: Heine A]]
-	[[Category: Heine, A]]	+	[[Category: Klebe G]]
-	[[Category: Klebe, G]]	+	[[Category: Wienen-Schmidt B]]
-	[[Category: Wienen-Schmidt, B]]	+
-	~~[[Category: 3x-phosphorylated]]~~	+
-	~~[[Category: Cocrystal]]~~	+
-	~~[[Category: Fasudil-derivative]]~~	+
-	~~[[Category: Inhibition]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Ligand 10]]~~	+
-	~~[[Category: Pka]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:07, 5 August 2020

OCA — Wed, 05 Aug 2020 07:07:17 GMT

←Older revision		Revision as of 07:07, 5 August 2020
Line 1:		Line 1:

	==Cocrystal structure of cAMP-dependent Protein Kinase (PKA) in complex with open-chain Fasudil-derivative (Ligand 04)==		==Cocrystal structure of cAMP-dependent Protein Kinase (PKA) in complex with open-chain Fasudil-derivative (Ligand 04)==
-	<StructureSection load='5lcr' size='340' side='right' caption='[[5lcr]], [[Resolution\|resolution]] 1.56Å' scene=''>	+	<StructureSection load='5lcr' size='340' side='right'caption='[[5lcr]], [[Resolution\|resolution]] 1.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lcr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCR OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5LCR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lcr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LCR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6TX:2-[isoquinolin-5-ylsulfonyl(propyl)amino]ethylazanium'>6TX</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6TX:2-[isoquinolin-5-ylsulfonyl(propyl)amino]ethylazanium'>6TX</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5lcp\|5lcp]], [[5lcq\|5lcq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5lcp\|5lcp]], [[5lcq\|5lcq]]</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=5lcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcr OCA], [http://pdbe.org/5lcr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lcr RCSB], [http://www.ebi.ac.uk/pdbsum/5lcr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcr 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=5lcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcr OCA], [http://pdbe.org/5lcr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lcr RCSB], [http://www.ebi.ac.uk/pdbsum/5lcr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcr ProSAT]</span></td></tr>
	</table>		</table>
	== 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/IPKA_HUMAN IPKA_HUMAN]] Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.		[[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/IPKA_HUMAN IPKA_HUMAN]] Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
		+
		+	==See Also==
		+	*[[CAMP-dependent protein kinase 3D structures\|CAMP-dependent protein kinase 3D structures]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: CAMP-dependent protein kinase]]		[[Category: CAMP-dependent protein kinase]]
	[[Category: Heine, A]]		[[Category: Heine, A]]

OCA at 06:45, 17 January 2018

OCA — Wed, 17 Jan 2018 06:45:18 GMT

←Older revision		Revision as of 06:45, 17 January 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5lcr is ~~ON HOLD until Paper Publication~~	+	==Cocrystal structure of cAMP-dependent Protein Kinase (PKA) in complex with open-chain Fasudil-derivative (Ligand 04)==
-		+	<StructureSection load='5lcr' size='340' side='right' caption='[[5lcr]], [[Resolution\|resolution]] 1.56Å' scene=''>
-	~~Authors~~: ~~Wienen~~-~~Schmidt~~, B., ~~Heine~~, A., ~~Klebe~~, G.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5lcr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LCR FirstGlance]. <br>
-	~~Description~~: ~~Cocrystal structure~~ of ~~cAMP~~-~~dependent Protein Kinase (PKA)~~ in complex with ~~open~~-~~chain Fasudil~~-~~derivative~~ (~~Ligand 04~~)	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6TX:2-[isoquinolin-5-ylsulfonyl(propyl)amino]ethylazanium'>6TX</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5lcp\|5lcp]], [[5lcq\|5lcq]]</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=5lcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcr OCA], [http://pdbe.org/5lcr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lcr RCSB], [http://www.ebi.ac.uk/pdbsum/5lcr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcr 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). [[http://www.uniprot.org/uniprot/IPKA_HUMAN IPKA_HUMAN]] Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: CAMP-dependent protein kinase]]
	[[Category: Heine, A]]		[[Category: Heine, A]]
		+	[[Category: Klebe, G]]
	[[Category: Wienen-Schmidt, B]]		[[Category: Wienen-Schmidt, B]]
-	[[Category: ~~Klebe, G~~]]	+	[[Category: 3x-phosphorylated]]
		+	[[Category: Cocrystal]]
		+	[[Category: Fasudil-derivative]]
		+	[[Category: Inhibition]]
		+	[[Category: Kinase]]
		+	[[Category: Ligand 10]]
		+	[[Category: Pka]]
		+	[[Category: Transferase]]

OCA at 10:50, 27 September 2017

OCA — Wed, 27 Sep 2017 10:50:13 GMT

←Older revision		Revision as of 10:50, 27 September 2017
Line 3:		Line 3:
	The entry 5lcr is ON HOLD until Paper Publication		The entry 5lcr is ON HOLD until Paper Publication

-	Authors: Wienen, B~~., Jonker, H., Gerber, H.-D~~., Heine, A~~., Schwalbe, H~~., Klebe, G.	+	Authors: Wienen-Schmidt, B., Heine, A., Klebe, G.

-	Description: Cocrystal structure of cAMP-dependent Protein Kinase (PKA) in complex with open-~~chained~~ Fasudil-derivative (Ligand 10)	+	Description: Cocrystal structure of cAMP-dependent Protein Kinase (PKA) in complex with open-chain Fasudil-derivative (Ligand 04)
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Jonker, H]]
	[[Category: Heine, A]]		[[Category: Heine, A]]
-	[[Category: Wienen, B]]	+	[[Category: Wienen-Schmidt, B]]
-	~~[[Category: Schwalbe, H]]~~	+
-	~~[[Category: Gerber, H.-D~~]]	+
	[[Category: Klebe, G]]		[[Category: Klebe, G]]

OCA at 10:36, 9 March 2017

OCA — Thu, 09 Mar 2017 10:36:31 GMT

←Older revision		Revision as of 10:36, 9 March 2017
Line 8:		Line 8:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Jonker, H]]		[[Category: Jonker, H]]
		+	[[Category: Heine, A]]
	[[Category: Wienen, B]]		[[Category: Wienen, B]]
		+	[[Category: Schwalbe, H]]
	[[Category: Gerber, H.-D]]		[[Category: Gerber, H.-D]]
	[[Category: Klebe, G]]		[[Category: Klebe, G]]
-	[[Category: Heine, A]]
-	[[Category: Schwalbe, H]]

OCA: Protected "5lcr" [edit=sysop:move=sysop]

OCA — Wed, 13 Jul 2016 00:59:15 GMT

Protected "5lcr" [edit=sysop:move=sysop]

←Older revision

Revision as of 00:59, 13 July 2016

OCA: New page: '''Unreleased structure''' The entry 5lcr is ON HOLD until Paper Publication Authors: Wienen, B., Jonker, H., Gerber, H.-D., Heine, A., Schwalbe, H., Klebe, G. Description: Cocrystal s...

OCA — Wed, 13 Jul 2016 00:59:14 GMT

New page: '''Unreleased structure''' The entry 5lcr is ON HOLD until Paper Publication Authors: Wienen, B., Jonker, H., Gerber, H.-D., Heine, A., Schwalbe, H., Klebe, G. Description: Cocrystal s...

New page

'''Unreleased structure'''

The entry 5lcr is ON HOLD until Paper Publication

Authors: Wienen, B., Jonker, H., Gerber, H.-D., Heine, A., Schwalbe, H., Klebe, G.

Description: Cocrystal structure of cAMP-dependent Protein Kinase (PKA) in complex with open-chained Fasudil-derivative (Ligand 10)
[[Category: Unreleased Structures]]
[[Category: Jonker, H]]
[[Category: Wienen, B]]
[[Category: Gerber, H.-D]]
[[Category: Klebe, G]]
[[Category: Heine, A]]
[[Category: Schwalbe, H]]