2xj2 - Revision history

OCA at 07:11, 1 May 2024

OCA — Wed, 01 May 2024 07:11:13 GMT

←Older revision		Revision as of 07:11, 1 May 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[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>		[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;">
-	== Publication Abstract from PubMed ==
-	A crystallographic fragment screen was carried out to identify starting points for the development of inhibitors of protein kinase Pim-1, a potential target for tumour therapy. All fragment hits identified via soaking in this study turned out to bind to the unusually hydrophobic pocket at the hinge region. The most potent fragments, two cinnamic acid derivatives (with a best IC(50) of 130 microM), additionally form a well defined hydrogen bond. The balance between hydrophobic and polar interactions makes these molecules good starting points for further optimization. Pim-2 inhibitors from a recently reported high-throughput screening campaign also feature a cinnamic acid moiety. Two of these Pim-2 inhibitors were synthesized, their potencies against Pim-1 were determined and their cocrystal structures were elucidated in order to determine to what degree the binding modes identified by fragment screening are conserved in optimized inhibitors. The structures show that the cinnamic acid moieties indeed adopt the same binding mode. Fragment screening thus correctly identified binding modes which are maintained when fragments are grown into larger and higher affinity inhibitors. The high-throughput screening-derived compound (E)-3-{3-[6-(4-aminocyclohexylamino)-pyrazin-2-yl]phenyl}acrylic acid (compound 1) is the most potent inhibitor of the cinnamic acid series for which the three-dimensional binding mode is known (IC(50) = 17 nM, K(d) = 28 nM). The structure reveals the molecular basis for the large gain in potency between the initial fragment hit and this optimized inhibitor.
-
-	A crystallographic fragment screen identifies cinnamic acid derivatives as starting points for potent Pim-1 inhibitors.,Schulz MN, Fanghanel J, Schafer M, Badock V, Briem H, Boemer U, Nguyen D, Husemann M, Hillig RC Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):156-66. Epub 2011, Feb 15. PMID:21358046<ref>PMID:21358046</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2xj2" style="background-color:#fffaf0;"></div>

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

OCA at 10:39, 16 August 2023

OCA — Wed, 16 Aug 2023 10:39:39 GMT

←Older revision		Revision as of 10:39, 16 August 2023
Line 3:		Line 3:
	<StructureSection load='2xj2' size='340' side='right'caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2xj2' size='340' side='right'caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xj2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XJ2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xj2]] 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=2XJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XJ2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=985:(2E)-3-{3~~-[~~6-(4-METHYL-1,4-DIAZEPAN-1-YL)PYRAZIN-2-YL~~]~~PHENYL}PROP-~~2~~-ENOIC+ACID'>985</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]] 2.2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=985:(2E)-3-{3-[6-(4-METHYL-1,4-DIAZEPAN-1-YL)PYRAZIN-2-YL]PHENYL}PROP-2-ENOIC+ACID'>985</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[~~[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;'>[[2bik\|2bik]]~~, ~~[[2xix\|2xix~~]], [[1ywv\|1ywv]], [[2bzj\|2bzj]], [[2c3i\|2c3i]], [[1yxu\|1yxu]], [[2j2i\|2j2i]], [[1yxt\|1yxt]], [[2bzh\|2bzh]], [[1yxs\|1yxs]], [[1xqz\|1xqz]], [[1yi3\|1yi3]], [[1yxv\|1yxv]], [[2xiz\|2xiz]], [[1xr1\|1xr1]], [[2xiy\|2xiy]], [[2bil\|2bil]], [[1yhs\|1yhs]], [[1xws\|1xws]], [[1yxx\|1yxx]], [[2bzk\|2bzk]], [[2xj1\|2xj1]], [[2xj0\|2xj0]], [[1yi4\|1yi4]], [[2bzi\|2bzi]]</div></td></tr>	+
-	~~<tr id='gene~~'>~~<td class="sblockLbl"><b>[[Gene\|Gene:]]~~</b><~~/td><td class="sblockDat">PIM1 ([https://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~~'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [https://pdbe.org/2xj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [https://www.ebi.ac.uk/pdbsum/2xj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xj2 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=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [https://pdbe.org/2xj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [https://www.ebi.ac.uk/pdbsum/2xj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xj2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[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 30:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Badock V]]
-	[[Category: Badock, V]]	+	[[Category: Boemer U]]
-	[[Category: Boemer, U]]	+	[[Category: Briem H]]
-	[[Category: Briem, H]]	+	[[Category: Fanghanel J]]
-	[[Category: Fanghanel, J]]	+	[[Category: Hillig RC]]
-	[[Category: Hillig~~, R C~~]]	+	[[Category: Husemann M]]
-	[[Category: Husemann, M]]	+	[[Category: Nguyen D]]
-	[[Category: Nguyen, D]]	+	[[Category: Schafer M]]
-	[[Category: Schafer, M]]	+	[[Category: Schulz MN]]
-	[[Category: Schulz~~, M N]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Protein kinase fold]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:40, 10 November 2021

OCA — Wed, 10 Nov 2021 08:40:55 GMT

←Older revision		Revision as of 08:40, 10 November 2021
Line 1:		Line 1:

	==Protein kinase Pim-1 in complex with small molecule inhibitor==		==Protein kinase Pim-1 in complex with small molecule inhibitor==
-	<StructureSection load='2xj2' size='340' side='right' caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='2xj2' size='340' side='right'caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xj2]] 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=2XJ2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2XJ2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xj2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XJ2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=985:(2E)-3-{3-[6-(4-METHYL-1,4-DIAZEPAN-1-YL)PYRAZIN-2-YL]PHENYL}PROP-2-ENOIC+ACID'>985</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=985:(2E)-3-{3-[6-(4-METHYL-1,4-DIAZEPAN-1-YL)PYRAZIN-2-YL]PHENYL}PROP-2-ENOIC+ACID'>985</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='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">[[2bik\|2bik]], [[2xix\|2xix]], [[1ywv\|1ywv]], [[2bzj\|2bzj]], [[2c3i\|2c3i]], [[1yxu\|1yxu]], [[2j2i\|2j2i]], [[1yxt\|1yxt]], [[2bzh\|2bzh]], [[1yxs\|1yxs]], [[1xqz\|1xqz]], [[1yi3\|1yi3]], [[1yxv\|1yxv]], [[2xiz\|2xiz]], [[1xr1\|1xr1]], [[2xiy\|2xiy]], [[2bil\|2bil]], [[1yhs\|1yhs]], [[1xws\|1xws]], [[1yxx\|1yxx]], [[2bzk\|2bzk]], [[2xj1\|2xj1]], [[2xj0\|2xj0]], [[1yi4\|1yi4]], [[2bzi\|2bzi]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bik\|2bik]], [[2xix\|2xix]], [[1ywv\|1ywv]], [[2bzj\|2bzj]], [[2c3i\|2c3i]], [[1yxu\|1yxu]], [[2j2i\|2j2i]], [[1yxt\|1yxt]], [[2bzh\|2bzh]], [[1yxs\|1yxs]], [[1xqz\|1xqz]], [[1yi3\|1yi3]], [[1yxv\|1yxv]], [[2xiz\|2xiz]], [[1xr1\|1xr1]], [[2xiy\|2xiy]], [[2bil\|2bil]], [[1yhs\|1yhs]], [[1xws\|1xws]], [[1yxx\|1yxx]], [[2bzk\|2bzk]], [[2xj1\|2xj1]], [[2xj0\|2xj0]], [[1yi4\|1yi4]], [[2bzi\|2bzi]]</div></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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIM1 ([https://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'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://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=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [~~http~~://pdbe.org/2xj2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2xj2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2xj2 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=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [https://pdbe.org/2xj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [https://www.ebi.ac.uk/pdbsum/2xj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xj2 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 24:

	==See Also==		==See Also==
-	*[[~~Proto-oncogene serine~~/threonine-protein kinase\|~~Proto-oncogene serine~~/threonine-protein kinase]]	+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
		+	*[[3D structures of pim-1\|3D structures of pim-1]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Badock, V]]		[[Category: Badock, V]]

OCA at 09:35, 3 October 2018

OCA — Wed, 03 Oct 2018 09:35:32 GMT

←Older revision		Revision as of 09:35, 3 October 2018
Line 1:		Line 1:

-	==~~PROTEIN KINASE PIM~~-1 ~~IN COMPLEX WITH SMALL MOLECULE INHIBITOR~~==	+	==Protein kinase Pim-1 in complex with small molecule inhibitor==
	<StructureSection load='2xj2' size='340' side='right' caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2xj2' size='340' side='right' caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 16:19, 4 August 2016

OCA — Thu, 04 Aug 2016 16:19:29 GMT

←Older revision		Revision as of 16:19, 4 August 2016
Line 1:		Line 1:
		+
	==PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR==		==PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR==
	<StructureSection load='2xj2' size='340' side='right' caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2xj2' size='340' side='right' caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xj2]] 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=2XJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XJ2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xj2]] 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=2XJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XJ2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=985:(2E)-3-{3-[6-(4-METHYL-1,4-DIAZEPAN-1-YL)PYRAZIN-2-YL]PHENYL}PROP-2-ENOIC+ACID'>985</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=985:(2E)-3-{3-[6-(4-METHYL-1,4-DIAZEPAN-1-YL)PYRAZIN-2-YL]PHENYL}PROP-2-ENOIC+ACID'>985</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='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">[[2bik\|2bik]], [[2xix\|2xix]], [[1ywv\|1ywv]], [[2bzj\|2bzj]], [[2c3i\|2c3i]], [[1yxu\|1yxu]], [[2j2i\|2j2i]], [[1yxt\|1yxt]], [[2bzh\|2bzh]], [[1yxs\|1yxs]], [[1xqz\|1xqz]], [[1yi3\|1yi3]], [[1yxv\|1yxv]], [[2xiz\|2xiz]], [[1xr1\|1xr1]], [[2xiy\|2xiy]], [[2bil\|2bil]], [[1yhs\|1yhs]], [[1xws\|1xws]], [[1yxx\|1yxx]], [[2bzk\|2bzk]], [[2xj1\|2xj1]], [[2xj0\|2xj0]], [[1yi4\|1yi4]], [[2bzi\|2bzi]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2bik\|2bik]], [[2xix\|2xix]], [[1ywv\|1ywv]], [[2bzj\|2bzj]], [[2c3i\|2c3i]], [[1yxu\|1yxu]], [[2j2i\|2j2i]], [[1yxt\|1yxt]], [[2bzh\|2bzh]], [[1yxs\|1yxs]], [[1xqz\|1xqz]], [[1yi3\|1yi3]], [[1yxv\|1yxv]], [[2xiz\|2xiz]], [[1xr1\|1xr1]], [[2xiy\|2xiy]], [[2bil\|2bil]], [[1yhs\|1yhs]], [[1xws\|1xws]], [[1yxx\|1yxx]], [[2bzk\|2bzk]], [[2xj1\|2xj1]], [[2xj0\|2xj0]], [[1yi4\|1yi4]], [[2bzi\|2bzi]]</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 ~~Homo sapiens~~])</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=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [http://www.ebi.ac.uk/pdbsum/2xj2 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=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [http://pdbe.org/2xj2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [http://www.ebi.ac.uk/pdbsum/2xj2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xj2 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 2xj2" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Badock, V]]		[[Category: Badock, V]]

OCA at 10:56, 25 December 2014

OCA — Thu, 25 Dec 2014 10:56:28 GMT

←Older revision		Revision as of 10:56, 25 December 2014
Line 10:		Line 10:
	<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=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [http://www.ebi.ac.uk/pdbsum/2xj2 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=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [http://www.ebi.ac.uk/pdbsum/2xj2 PDBsum]</span></td></tr>
	</table>		</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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:59, 12 November 2014

OCA — Wed, 12 Nov 2014 07:59:35 GMT

←Older revision		Revision as of 07:59, 12 November 2014
Line 1:		Line 1:
-	[[~~Image:~~2xj2.~~png~~\|~~left~~\|~~200px~~]]	+	==PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR==
		+	<StructureSection load='2xj2' size='340' side='right' caption='[[2xj2]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2xj2]] 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=2XJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XJ2 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=985:(2E)-3-{3-[6-(4-METHYL-1,4-DIAZEPAN-1-YL)PYRAZIN-2-YL]PHENYL}PROP-2-ENOIC+ACID'>985</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">[[2bik\|2bik]], [[2xix\|2xix]], [[1ywv\|1ywv]], [[2bzj\|2bzj]], [[2c3i\|2c3i]], [[1yxu\|1yxu]], [[2j2i\|2j2i]], [[1yxt\|1yxt]], [[2bzh\|2bzh]], [[1yxs\|1yxs]], [[1xqz\|1xqz]], [[1yi3\|1yi3]], [[1yxv\|1yxv]], [[2xiz\|2xiz]], [[1xr1\|1xr1]], [[2xiy\|2xiy]], [[2bil\|2bil]], [[1yhs\|1yhs]], [[1xws\|1xws]], [[1yxx\|1yxx]], [[2bzk\|2bzk]], [[2xj1\|2xj1]], [[2xj0\|2xj0]], [[1yi4\|1yi4]], [[2bzi\|2bzi]]</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 Homo sapiens])</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=2xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xj2 RCSB], [http://www.ebi.ac.uk/pdbsum/2xj2 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A crystallographic fragment screen was carried out to identify starting points for the development of inhibitors of protein kinase Pim-1, a potential target for tumour therapy. All fragment hits identified via soaking in this study turned out to bind to the unusually hydrophobic pocket at the hinge region. The most potent fragments, two cinnamic acid derivatives (with a best IC(50) of 130 microM), additionally form a well defined hydrogen bond. The balance between hydrophobic and polar interactions makes these molecules good starting points for further optimization. Pim-2 inhibitors from a recently reported high-throughput screening campaign also feature a cinnamic acid moiety. Two of these Pim-2 inhibitors were synthesized, their potencies against Pim-1 were determined and their cocrystal structures were elucidated in order to determine to what degree the binding modes identified by fragment screening are conserved in optimized inhibitors. The structures show that the cinnamic acid moieties indeed adopt the same binding mode. Fragment screening thus correctly identified binding modes which are maintained when fragments are grown into larger and higher affinity inhibitors. The high-throughput screening-derived compound (E)-3-{3-[6-(4-aminocyclohexylamino)-pyrazin-2-yl]phenyl}acrylic acid (compound 1) is the most potent inhibitor of the cinnamic acid series for which the three-dimensional binding mode is known (IC(50) = 17 nM, K(d) = 28 nM). The structure reveals the molecular basis for the large gain in potency between the initial fragment hit and this optimized inhibitor.

-	~~{{STRUCTURE_2xj2\| PDB=2xj2 \| SCENE= }}~~	+	A crystallographic fragment screen identifies cinnamic acid derivatives as starting points for potent Pim-1 inhibitors.,Schulz MN, Fanghanel J, Schafer M, Badock V, Briem H, Boemer U, Nguyen D, Husemann M, Hillig RC Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):156-66. Epub 2011, Feb 15. PMID:21358046<ref>PMID:21358046</ref>

-	~~===PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_21358046}}~~	+	==See Also==
-		+	*[[Proto-oncogene serine/threonine-protein kinase\|Proto-oncogene serine/threonine-protein kinase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~2xj2]] 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=2XJ2 OCA~~].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:021358046<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Badock, V.]]	+	[[Category: Badock, V]]
-	[[Category: Boemer, U.]]	+	[[Category: Boemer, U]]
-	[[Category: Briem, H.]]	+	[[Category: Briem, H]]
-	[[Category: Fanghanel, J.]]	+	[[Category: Fanghanel, J]]
-	[[Category: Hillig, R C.]]	+	[[Category: Hillig, R C]]
-	[[Category: Husemann, M.]]	+	[[Category: Husemann, M]]
-	[[Category: Nguyen, D.]]	+	[[Category: Nguyen, D]]
-	[[Category: Schafer, M.]]	+	[[Category: Schafer, M]]
-	[[Category: Schulz, M N.]]	+	[[Category: Schulz, M N]]
	[[Category: Phosphorylation]]		[[Category: Phosphorylation]]
	[[Category: Protein kinase fold]]		[[Category: Protein kinase fold]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 13:23, 6 February 2013

OCA — Wed, 06 Feb 2013 13:23:20 GMT

←Older revision		Revision as of 13:23, 6 February 2013
Line 1:		Line 1:
	[[Image:2xj2.png\|left\|200px]]		[[Image:2xj2.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2xj2", 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_2xj2\| PDB=2xj2 \| SCENE= }}		{{STRUCTURE_2xj2\| PDB=2xj2 \| SCENE= }}

	===PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR===		===PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21358046}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21358046 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_21358046}}		{{ABSTRACT_PUBMED_21358046}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~21358046~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021358046</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
Line 34:		Line 23:
	[[Category: Schafer, M.]]		[[Category: Schafer, M.]]
	[[Category: Schulz, M N.]]		[[Category: Schulz, M N.]]
		+	[[Category: Phosphorylation]]
		+	[[Category: Protein kinase fold]]
		+	[[Category: Transferase]]

OCA at 07:22, 16 March 2011

OCA — Wed, 16 Mar 2011 07:22:35 GMT

←Older revision		Revision as of 07:22, 16 March 2011
Line 1:		Line 1:
-	[[Image:2xj2.~~jpg~~\|left\|200px]]	+	[[Image:2xj2.png\|left\|200px]]

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	===PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR===		===PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21358046}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21358046 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21358046}}

	==About this Structure==		==About this Structure==
-	[[2xj2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermomicrobium_roseum Thermomicrobium roseum~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XJ2 OCA].	+	[[2xj2]] 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=2XJ2 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:21358046</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Thermomicrobium roseum]]
	[[Category: Badock, V.]]		[[Category: Badock, V.]]
	[[Category: Boemer, U.]]		[[Category: Boemer, U.]]

OCA: Protected "2xj2" [edit=sysop:move=sysop]

OCA — Wed, 23 Feb 2011 09:54:44 GMT

Protected "2xj2" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:54, 23 February 2011