4daw - Revision history

OCA at 14:30, 14 March 2024

OCA — Thu, 14 Mar 2024 14:30:19 GMT

←Older revision		Revision as of 14:30, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DAW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DAW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</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]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</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=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [https://pdbe.org/4daw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [https://www.ebi.ac.uk/pdbsum/4daw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4daw 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=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [https://pdbe.org/4daw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [https://www.ebi.ac.uk/pdbsum/4daw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4daw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PAK1_HUMAN PAK1_HUMAN]] Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2.<ref>PMID:8805275</ref> <ref>PMID:9395435</ref> <ref>PMID:9032240</ref> <ref>PMID:9528787</ref> <ref>PMID:10551809</ref> <ref>PMID:11733498</ref> <ref>PMID:12624090</ref> <ref>PMID:12876277</ref> <ref>PMID:14585966</ref> <ref>PMID:15611088</ref> <ref>PMID:15831477</ref> <ref>PMID:16278681</ref> <ref>PMID:17726028</ref> <ref>PMID:17989089</ref> <ref>PMID:22669945</ref>	+	[https://www.uniprot.org/uniprot/PAK1_HUMAN PAK1_HUMAN] Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2.<ref>PMID:8805275</ref> <ref>PMID:9395435</ref> <ref>PMID:9032240</ref> <ref>PMID:9528787</ref> <ref>PMID:10551809</ref> <ref>PMID:11733498</ref> <ref>PMID:12624090</ref> <ref>PMID:12876277</ref> <ref>PMID:14585966</ref> <ref>PMID:15611088</ref> <ref>PMID:15831477</ref> <ref>PMID:16278681</ref> <ref>PMID:17726028</ref> <ref>PMID:17989089</ref> <ref>PMID:22669945</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Better fit, less effort: An easy-to-synthesize ruthenium phthalimide complex (tan-colored carbon atoms in the picture) was designed to bind within the active site of the p21-activated kinase 1 in a novel fashion that differs from that of the previously established staurosporine-inspired metallopyridocarbazoles (gray-colored carbon atoms).	+
-		+
-	The Art of Filling Protein Pockets Efficiently with Octahedral Metal Complexes.,Blanck S, Maksimoska J, Baumeister J, Harms K, Marmorstein R, Meggers E Angew Chem Int Ed Engl. 2012 Mar 1. doi: 10.1002/anie.201108865. PMID:22383326<ref>PMID:22383326</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4daw" style="background-color:#fffaf0;"></div~~>	+

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

OCA at 08:09, 21 September 2022

OCA — Wed, 21 Sep 2022 08:09:28 GMT

←Older revision		Revision as of 08:09, 21 September 2022
Line 1:		Line 1:

	==Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex==		==Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex==
-	<StructureSection load='4daw' size='340' side='right' caption='[[4daw]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4daw' size='340' side='right'caption='[[4daw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DAW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DAW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</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=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=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [https://pdbe.org/4daw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [https://www.ebi.ac.uk/pdbsum/4daw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4daw ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [~~http~~://pdbe.org/4daw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4daw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4daw ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PAK1_HUMAN PAK1_HUMAN]] Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2.<ref>PMID:8805275</ref> <ref>PMID:9395435</ref> <ref>PMID:9032240</ref> <ref>PMID:9528787</ref> <ref>PMID:10551809</ref> <ref>PMID:11733498</ref> <ref>PMID:12624090</ref> <ref>PMID:12876277</ref> <ref>PMID:14585966</ref> <ref>PMID:15611088</ref> <ref>PMID:15831477</ref> <ref>PMID:16278681</ref> <ref>PMID:17726028</ref> <ref>PMID:17989089</ref> <ref>PMID:22669945</ref>	+	[[https://www.uniprot.org/uniprot/PAK1_HUMAN PAK1_HUMAN]] Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2.<ref>PMID:8805275</ref> <ref>PMID:9395435</ref> <ref>PMID:9032240</ref> <ref>PMID:9528787</ref> <ref>PMID:10551809</ref> <ref>PMID:11733498</ref> <ref>PMID:12624090</ref> <ref>PMID:12876277</ref> <ref>PMID:14585966</ref> <ref>PMID:15611088</ref> <ref>PMID:15831477</ref> <ref>PMID:16278681</ref> <ref>PMID:17726028</ref> <ref>PMID:17989089</ref> <ref>PMID:22669945</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]	+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Non-specific serine/threonine protein kinase~~]]	+	[[Category: Large Structures]]
-	[[Category: Maksimoska, J]]	+	[[Category: Maksimoska J]]
-	[[Category: Marmorstein, R]]	+	[[Category: Marmorstein R]]
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Serine/threonine kinase]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 06:01, 5 August 2016

OCA — Fri, 05 Aug 2016 06:01:34 GMT

←Older revision		Revision as of 06:01, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex==		==Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex==
	<StructureSection load='4daw' size='340' side='right' caption='[[4daw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4daw' size='340' side='right' caption='[[4daw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DAW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DAW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><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=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [http://www.ebi.ac.uk/pdbsum/4daw 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=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [http://pdbe.org/4daw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [http://www.ebi.ac.uk/pdbsum/4daw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4daw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4daw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Maksimoska, J]]		[[Category: Maksimoska, J]]

OCA at 16:21, 25 December 2014

OCA — Thu, 25 Dec 2014 16:21:32 GMT

←Older revision		Revision as of 16:21, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DAW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DAW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><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=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [http://www.ebi.ac.uk/pdbsum/4daw 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=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [http://www.ebi.ac.uk/pdbsum/4daw PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PAK1_HUMAN PAK1_HUMAN]] Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2.<ref>PMID:8805275</ref> <ref>PMID:9395435</ref> <ref>PMID:9032240</ref> <ref>PMID:9528787</ref> <ref>PMID:10551809</ref> <ref>PMID:11733498</ref> <ref>PMID:12624090</ref> <ref>PMID:12876277</ref> <ref>PMID:14585966</ref> <ref>PMID:15611088</ref> <ref>PMID:15831477</ref> <ref>PMID:16278681</ref> <ref>PMID:17726028</ref> <ref>PMID:17989089</ref> <ref>PMID:22669945</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 28:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Maksimoska, J.]]	+	[[Category: Maksimoska, J]]
-	[[Category: Marmorstein, R.]]	+	[[Category: Marmorstein, R]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Phosphorylation]]		[[Category: Phosphorylation]]
	[[Category: Serine/threonine kinase]]		[[Category: Serine/threonine kinase]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 08:02, 5 June 2014

OCA — Thu, 05 Jun 2014 08:02:56 GMT

←Older revision		Revision as of 08:02, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~4daw.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex==
		+	<StructureSection load='4daw' size='340' side='right' caption='[[4daw]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4daw]] 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=4DAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DAW FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0H2:[1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)RUTHENIUM'>0H2</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4daw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4daw RCSB], [http://www.ebi.ac.uk/pdbsum/4daw PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Better fit, less effort: An easy-to-synthesize ruthenium phthalimide complex (tan-colored carbon atoms in the picture) was designed to bind within the active site of the p21-activated kinase 1 in a novel fashion that differs from that of the previously established staurosporine-inspired metallopyridocarbazoles (gray-colored carbon atoms).

-	~~<!--~~	+	The Art of Filling Protein Pockets Efficiently with Octahedral Metal Complexes.,Blanck S, Maksimoska J, Baumeister J, Harms K, Marmorstein R, Meggers E Angew Chem Int Ed Engl. 2012 Mar 1. doi: 10.1002/anie.201108865. PMID:22383326<ref>PMID:22383326</ref>
-	The ~~line below this paragraph~~, ~~containing "STRUCTURE_4daw"~~, ~~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_4daw\| PDB=4daw \| SCENE= }}~~	+

-	~~===Crystal structure~~ of ~~PAK1 kinase domain with~~ the ~~ruthenium phthalimide complex===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	~~<!--~~	+	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22383326}}, adds the Publication Abstract to the page~~	+	== References ==
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 22383326 is the PubMed ID number.~~	+	<references/>
-	~~-->~~	+	__TOC__
-	~~{{ABSTRACT_PUBMED_22383326}}~~	+	</StructureSection>
-		+
-	==~~About this Structure~~==	+
-	[[~~4daw]] 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=4DAW OCA~~].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022383326<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]

OCA at 04:56, 30 May 2012

OCA — Wed, 30 May 2012 04:56:13 GMT

←Older revision		Revision as of 04:56, 30 May 2012
Line 1:		Line 1:
-	[[Image:4daw.~~jpg~~\|left\|200px]]	+	[[Image:4daw.png\|left\|200px]]

	<!--		<!--

OCA at 06:34, 14 March 2012

OCA — Wed, 14 Mar 2012 06:34:27 GMT

←Older revision		Revision as of 06:34, 14 March 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4daw.jpg\|left\|200px]]

-	The ~~entry 4daw~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_4daw", 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_4daw\| PDB=4daw \| SCENE= }}

-	~~Authors: Maksimoska, J., Marmorstein, R.~~	+	===Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex===

-	~~Description~~: ~~Crystal~~ structure ~~of PAK1 kinase domain~~ with ~~the ruthenium phthalimide~~ complex	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22383326}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22383326 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22383326}}
		+
		+	==About this Structure==
		+	[[4daw]] 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=4DAW OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022383326</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Maksimoska, J.]]
		+	[[Category: Marmorstein, R.]]
		+	[[Category: Atp-binding]]
		+	[[Category: Phosphorylation]]
		+	[[Category: Serine/threonine kinase]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 06:09, 8 February 2012

OCA — Wed, 08 Feb 2012 06:09:51 GMT

←Older revision		Revision as of 06:09, 8 February 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Maksimoska, J., Marmorstein, R.		Authors: Maksimoska, J., Marmorstein, R.

	Description: Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex		Description: Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex

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

OCA — Wed, 25 Jan 2012 06:10:00 GMT

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

←Older revision

Revision as of 06:10, 25 January 2012

OCA: New page: '''Unreleased structure''' The entry 4daw is ON HOLD Authors: Maksimoska, J., Marmorstein, R. Description: Crystal structure of PAK1 kinase domain with the ruthenium phthalimide comple...

OCA — Wed, 25 Jan 2012 06:09:59 GMT

New page: '''Unreleased structure''' The entry 4daw is ON HOLD Authors: Maksimoska, J., Marmorstein, R. Description: Crystal structure of PAK1 kinase domain with the ruthenium phthalimide comple...

New page

'''Unreleased structure'''

The entry 4daw is ON HOLD

Authors: Maksimoska, J., Marmorstein, R.

Description: Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex