4xh6 - Revision history

OCA at 15:27, 8 November 2023

OCA — Wed, 08 Nov 2023 15:27:57 GMT

←Older revision		Revision as of 15:27, 8 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4xh6]] 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=4XH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XH6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4xh6]] 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=4XH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XH6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HUL:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-6-METHOXY-4H-CHROMEN-4-ONE'>HUL</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.04Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HUL:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-6-METHOXY-4H-CHROMEN-4-ONE'>HUL</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=4xh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh6 OCA], [https://pdbe.org/4xh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xh6 RCSB], [https://www.ebi.ac.uk/pdbsum/4xh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh6 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=4xh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh6 OCA], [https://pdbe.org/4xh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xh6 RCSB], [https://www.ebi.ac.uk/pdbsum/4xh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh6 ProSAT]</span></td></tr>
	</table>		</table>
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4xh6" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4xh6" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:58, 19 April 2023

OCA — Wed, 19 Apr 2023 09:58:49 GMT

←Older revision		Revision as of 09:58, 19 April 2023
Line 3:		Line 3:
	<StructureSection load='4xh6' size='340' side='right'caption='[[4xh6]], [[Resolution\|resolution]] 2.04Å' scene=''>		<StructureSection load='4xh6' size='340' side='right'caption='[[4xh6]], [[Resolution\|resolution]] 2.04Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4xh6]] 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=4XH6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4XH6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4xh6]] 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=4XH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XH6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HUL:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-6-METHOXY-4H-CHROMEN-4-ONE'>HUL</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HUL:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-6-METHOXY-4H-CHROMEN-4-ONE'>HUL</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4xh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh6 OCA], [https://pdbe.org/4xh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xh6 RCSB], [https://www.ebi.ac.uk/pdbsum/4xh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh6 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/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=4xh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh6 OCA], [~~http~~://pdbe.org/4xh6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4xh6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4xh6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh6 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN]] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>	+	[https://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Chang C-I]]
-	[[Category: Chang, C I]]	+	[[Category: Su M-Y]]
-	[[Category: Su, M Y]]	+
-	~~[[Category: Hispidulin]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Pim1]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 08:39, 5 February 2020

OCA — Wed, 05 Feb 2020 08:39:16 GMT

←Older revision		Revision as of 08:39, 5 February 2020
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4xh6" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4xh6" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Proto-oncogene serine/threonine-protein kinase\|Proto-oncogene serine/threonine-protein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:25, 29 May 2019

OCA — Wed, 29 May 2019 07:25:57 GMT

←Older revision		Revision as of 07:25, 29 May 2019
Line 1:		Line 1:
		+
	==Crystal structure of proto-oncogene kinase Pim1 bound to hispidulin==		==Crystal structure of proto-oncogene kinase Pim1 bound to hispidulin==
-	<StructureSection load='4xh6' size='340' side='right' caption='[[4xh6]], [[Resolution\|resolution]] 2.04Å' scene=''>	+	<StructureSection load='4xh6' size='340' side='right'caption='[[4xh6]], [[Resolution\|resolution]] 2.04Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4xh6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XH6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XH6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4xh6]] 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=4XH6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XH6 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HUL:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-6-METHOXY-4H-CHROMEN-4-ONE'>HUL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HUL:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-6-METHOXY-4H-CHROMEN-4-ONE'>HUL</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIM1 ([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=4xh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xh6 RCSB], [http://www.ebi.ac.uk/pdbsum/4xh6 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=4xh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh6 OCA], [http://pdbe.org/4xh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xh6 RCSB], [http://www.ebi.ac.uk/pdbsum/4xh6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4xh6" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Proto-oncogene serine/threonine-protein kinase\|Proto-oncogene serine/threonine-protein kinase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Chang, C I]]		[[Category: Chang, C I]]

OCA at 13:27, 26 August 2015

OCA — Wed, 26 Aug 2015 13:27:27 GMT

←Older revision		Revision as of 13:27, 26 August 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of proto-oncogene kinase Pim1 bound to hispidulin==
		+	<StructureSection load='4xh6' size='340' side='right' caption='[[4xh6]], [[Resolution\|resolution]] 2.04Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4xh6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XH6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XH6 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HUL:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-6-METHOXY-4H-CHROMEN-4-ONE'>HUL</scene></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=4xh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xh6 RCSB], [http://www.ebi.ac.uk/pdbsum/4xh6 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN]] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A new method is applied to synthesize hispidulin, a natural flavone with a broad spectrum of biological activities. Hispidulin exhibits inhibitory activity against the oncogenic protein kinase Pim-1. Crystallographic analysis of Pim-1 bound to hispidulin reveals a binding mode distinct from that of quercetin, suggesting that the binding potency of flavonoids is determined by their hydrogen-bonding interactions with the hinge region of the kinase. Overall, this work may facilitate construction of a library of hispidulin-derived compounds for investigating the structure-activity relationship of flavone-based Pim-1 inhibitors.

-	~~The entry 4xh6 is ON HOLD until Paper Publication~~	+	Total Synthesis of Hispidulin and the Structural Basis for Its Inhibition of Proto-oncogene Kinase Pim-1.,Chao SW, Su MY, Chiou LC, Chen LC, Chang CI, Huang WJ J Nat Prod. 2015 Aug 14. PMID:26275107<ref>PMID:26275107</ref>

-	~~Authors: Su~~, M.-Y.~~, Chang, C.-I~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Crystal structure of proto-oncogene kinase Pim1 bound to hispidulin~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
-	[[Category: Chang, C.-I]]	+	__TOC__
-	[[Category: Su, M.-Y]]	+	</StructureSection>
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Chang, C I]]
		+	[[Category: Su, M Y]]
		+	[[Category: Hispidulin]]
		+	[[Category: Inhibitor]]
		+	[[Category: Kinase]]
		+	[[Category: Pim1]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA: Protected "4xh6" [edit=sysop:move=sysop]

OCA — Wed, 14 Jan 2015 12:42:09 GMT

Protected "4xh6" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:42, 14 January 2015

OCA: New page: '''Unreleased structure''' The entry 4xh6 is ON HOLD until Paper Publication Authors: Su, M.-Y., Chang, C.-I. Description: Crystal structure of proto-oncogene kinase Pim1 bound to hisp...

OCA — Wed, 14 Jan 2015 12:42:08 GMT

New page: '''Unreleased structure''' The entry 4xh6 is ON HOLD until Paper Publication Authors: Su, M.-Y., Chang, C.-I. Description: Crystal structure of proto-oncogene kinase Pim1 bound to hisp...

New page

'''Unreleased structure'''

The entry 4xh6 is ON HOLD until Paper Publication

Authors: Su, M.-Y., Chang, C.-I.

Description: Crystal structure of proto-oncogene kinase Pim1 bound to hispidulin
[[Category: Unreleased Structures]]
[[Category: Chang, C.-I]]
[[Category: Su, M.-Y]]