4o0v - Revision history

OCA at 08:50, 18 January 2023

OCA — Wed, 18 Jan 2023 08:50:57 GMT

←Older revision		Revision as of 08:50, 18 January 2023
Line 1:		Line 1:

	==Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors==		==Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors==
-	<StructureSection load='4o0v' size='340' side='right' caption='[[4o0v]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='4o0v' size='340' side='right'caption='[[4o0v]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o0v]] 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=4O0V OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4O0V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o0v]] 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=4O0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0V FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OL:1-({1-(2-AMINOPYRIMIDIN-4-YL)-2-[(2-METHOXYETHYL)AMINO]-1H-BENZIMIDAZOL-6-YL}ETHYNYL)CYCLOHEXANOL'>2OL</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2OL:1-({1-(2-AMINOPYRIMIDIN-4-YL)-2-[(2-METHOXYETHYL)AMINO]-1H-BENZIMIDAZOL-6-YL}ETHYNYL)CYCLOHEXANOL'>2OL</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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~~></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=4o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0v OCA], [https://pdbe.org/4o0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0v RCSB], [https://www.ebi.ac.uk/pdbsum/4o0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0v ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0r\|4o0r]], [[4o0t\|4o0t]], [[4o0x\|4o0x]], [[4o0y\|4o0y]]</td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK4, KIAA1142 ([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=4o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0v OCA], [~~http~~://pdbe.org/4o0v PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4o0v RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4o0v PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0v ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PAK4_HUMAN PAK4_HUMAN]] Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.<ref>PMID:11278822</ref> <ref>PMID:11313478</ref> <ref>PMID:14560027</ref> <ref>PMID:15660133</ref> <ref>PMID:20507994</ref> <ref>PMID:20805321</ref> <ref>PMID:20631255</ref>	+	[https://www.uniprot.org/uniprot/PAK4_HUMAN PAK4_HUMAN] Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.<ref>PMID:11278822</ref> <ref>PMID:11313478</ref> <ref>PMID:14560027</ref> <ref>PMID:15660133</ref> <ref>PMID:20507994</ref> <ref>PMID:20805321</ref> <ref>PMID:20631255</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		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: Rouge, L]]	+	[[Category: Rouge L]]
-	[[Category: Tam, C]]	+	[[Category: Tam C]]
-	[[Category: Wang, W]]	+	[[Category: Wang W]]
-	~~[[Category: Pak4]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 13:10, 4 August 2016

OCA — Thu, 04 Aug 2016 13:10:41 GMT

←Older revision		Revision as of 13:10, 4 August 2016
Line 1:		Line 1:
		+
	==Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors==		==Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors==
	<StructureSection load='4o0v' size='340' side='right' caption='[[4o0v]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='4o0v' size='340' side='right' caption='[[4o0v]], [[Resolution\|resolution]] 2.80Å' scene=''>
Line 8:		Line 9:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK4, KIAA1142 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK4, KIAA1142 ([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=4o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0v RCSB], [http://www.ebi.ac.uk/pdbsum/4o0v 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=4o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0v OCA], [http://pdbe.org/4o0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o0v RCSB], [http://www.ebi.ac.uk/pdbsum/4o0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0v ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	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 4o0v" style="background-color:#fffaf0;"></div>

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

OCA at 09:36, 25 December 2014

OCA — Thu, 25 Dec 2014 09:36:06 GMT

←Older revision		Revision as of 09:36, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4o0v\| PDB=4o0v \| SCENE= }}~~	+	==Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors==
-	===Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors===	+	<StructureSection load='4o0v' size='340' side='right' caption='[[4o0v]], [[Resolution\|resolution]] 2.80Å' scene=''>
-	{~~{ABSTRACT_PUBMED_24432870}~~}	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4o0v]] 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=4O0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0V FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OL:1-({1-(2-AMINOPYRIMIDIN-4-YL)-2-[(2-METHOXYETHYL)AMINO]-1H-BENZIMIDAZOL-6-YL}ETHYNYL)CYCLOHEXANOL'>2OL</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></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0r\|4o0r]], [[4o0t\|4o0t]], [[4o0x\|4o0x]], [[4o0y\|4o0y]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAK4, KIAA1142 ([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=4o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0v RCSB], [http://www.ebi.ac.uk/pdbsum/4o0v PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/PAK4_HUMAN PAK4_HUMAN]] Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.<ref>PMID:11278822</ref> <ref>PMID:11313478</ref> <ref>PMID:14560027</ref> <ref>PMID:15660133</ref> <ref>PMID:20507994</ref> <ref>PMID:20805321</ref> <ref>PMID:20631255</ref>		[[http://www.uniprot.org/uniprot/PAK4_HUMAN PAK4_HUMAN]] Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.<ref>PMID:11278822</ref> <ref>PMID:11313478</ref> <ref>PMID:14560027</ref> <ref>PMID:15660133</ref> <ref>PMID:20507994</ref> <ref>PMID:20805321</ref> <ref>PMID:20631255</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Structure-based methods were used to design a potent and highly selective group II p21-activated kinase (PAK) inhibitor with a novel binding mode, compound 17. Hydrophobic interactions within a lipophilic pocket past the methionine gatekeeper of group II PAKs approached by these type I 1/2 binders were found to be important for improving potency. A structure-based hypothesis and strategy for achieving selectivity over group I PAKs, and the broad kinome, based on unique flexibility of this lipophilic pocket, is presented. A concentration-dependent decrease in tumor cell migration and invasion in two triple-negative breast cancer cell lines was observed with compound 17.
		+
		+	Back Pocket Flexibility Provides Group II p21-Activated Kinase (PAK) Selectivity for Type I 1/2 Kinase Inhibitors.,Staben ST, Feng JA, Lyle K, Belvin M, Boggs J, Burch JD, Chua CC, Cui H, Dipasquale AG, Friedman LS, Heise C, Koeppen H, Kotey A, Mintzer R, Oh A, Roberts DA, Rouge L, Rudolph J, Tam C, Wang W, Xiao Y, Young A, Zhang Y, Hoeflich KP J Med Chem. 2014 Feb 4. PMID:24432870<ref>PMID:24432870</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4o0v]] is~~ a ~~1 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4O0V OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:024432870</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Rouge, L.]]	+	[[Category: Rouge, L]]
-	[[Category: Tam, C.]]	+	[[Category: Tam, C]]
-	[[Category: Wang, W.]]	+	[[Category: Wang, W]]
	[[Category: Pak4]]		[[Category: Pak4]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 05:06, 13 February 2014

OCA — Thu, 13 Feb 2014 05:06:23 GMT

←Older revision		Revision as of 05:06, 13 February 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4o0v\| PDB=4o0v \| SCENE= }}
		+	===Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors===
		+	{{ABSTRACT_PUBMED_24432870}}

-	~~The entry 4o0v is ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/PAK4_HUMAN PAK4_HUMAN]] Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.<ref>PMID:11278822</ref> <ref>PMID:11313478</ref> <ref>PMID:14560027</ref> <ref>PMID:15660133</ref> <ref>PMID:20507994</ref> <ref>PMID:20805321</ref> <ref>PMID:20631255</ref>

-	~~Authors~~: ~~Rouge, L~~.~~, Tam, C~~.~~, Wang, W~~.	+	==About this Structure==
		+	[[4o0v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0V OCA].

-	~~Description~~: ~~Back pocket flexibility provides~~ group-~~II PAK selectivity for type 1~~ kinase ~~inhibitors~~	+	==Reference==
		+	<ref group="xtra">PMID:024432870</ref><references group="xtra"/><references/>
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Rouge, L.]]
		+	[[Category: Tam, C.]]
		+	[[Category: Wang, W.]]
		+	[[Category: Pak4]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 06:45, 22 January 2014

OCA — Wed, 22 Jan 2014 06:45:29 GMT

←Older revision		Revision as of 06:45, 22 January 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4o0v is ON HOLD	+	The entry 4o0v is ON HOLD until Paper Publication

	Authors: Rouge, L., Tam, C., Wang, W.		Authors: Rouge, L., Tam, C., Wang, W.

	Description: Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors		Description: Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors

OCA: Protected "4o0v" [edit=sysop:move=sysop]

OCA — Wed, 25 Dec 2013 09:29:33 GMT

Protected "4o0v" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:29, 25 December 2013

OCA: New page: '''Unreleased structure''' The entry 4o0v is ON HOLD Authors: Rouge, L., Tam, C., Wang, W. Description: Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhi...

OCA — Wed, 25 Dec 2013 09:29:32 GMT

New page: '''Unreleased structure''' The entry 4o0v is ON HOLD Authors: Rouge, L., Tam, C., Wang, W. Description: Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhi...

New page

'''Unreleased structure'''

The entry 4o0v is ON HOLD

Authors: Rouge, L., Tam, C., Wang, W.

Description: Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors