4rv6 - Revision history

OCA at 17:56, 20 September 2023

OCA — Wed, 20 Sep 2023 17:56:35 GMT

←Older revision		Revision as of 17:56, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4rv6]] is a 4 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=4RV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RV6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4rv6]] is a 4 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=4RV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RV6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RPB:RUCAPARIB'>RPB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.19Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RPB:RUCAPARIB'>RPB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv6 OCA], [https://pdbe.org/4rv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rv6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv6 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=4rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv6 OCA], [https://pdbe.org/4rv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rv6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv6 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:29, 8 March 2023

OCA — Wed, 08 Mar 2023 08:29:24 GMT

←Older revision		Revision as of 08:29, 8 March 2023
Line 1:		Line 1:

	==Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib==		==Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib==
-	<StructureSection load='4rv6' size='340' side='right' caption='[[4rv6]], [[Resolution\|resolution]] 3.19Å' scene=''>	+	<StructureSection load='4rv6' size='340' side='right'caption='[[4rv6]], [[Resolution\|resolution]] 3.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rv6]] is a 4 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=4RV6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4RV6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4rv6]] is a 4 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=4RV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RV6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RPB:RUCAPARIB'>RPB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RPB:RUCAPARIB'>RPB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4und\|4und]], [[4uxb\|4uxb]], [[4r5w\|4r5w]], [[4r6e\|4r6e]]</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=4rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv6 OCA], [https://pdbe.org/4rv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rv6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv6 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADPRT, PARP1, PPOL ([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/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </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=4rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv6 OCA], [~~http~~://pdbe.org/4rv6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4rv6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4rv6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv6 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PARP1_HUMAN PARP1_HUMAN]] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.<ref>PMID:17177976</ref> <ref>PMID:18172500</ref> <ref>PMID:19344625</ref> <ref>PMID:19661379</ref>	+	[https://www.uniprot.org/uniprot/PARP1_HUMAN PARP1_HUMAN] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.<ref>PMID:17177976</ref> <ref>PMID:18172500</ref> <ref>PMID:19344625</ref> <ref>PMID:19661379</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==
-	*[[Poly (ADP-ribose) polymerase\|Poly (ADP-ribose) polymerase]]	+	*[[Poly(ADP-ribose) polymerase 3D structures\|Poly(ADP-ribose) polymerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Karlberg, T~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Schuler, H~~]]	+	[[Category: Karlberg T]]
-	[[Category: ~~Thorsell, A G~~]]	+	[[Category: Schuler H]]
-	[[Category: ~~Adp-ribosyl transferase]]~~	+	[[Category: Thorsell AG]]
-	~~[[Category: Adp-ribosylation]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 10:17, 5 September 2018

OCA — Wed, 05 Sep 2018 10:17:08 GMT

←Older revision		Revision as of 10:17, 5 September 2018
Line 12:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PARP1_HUMAN PARP1_HUMAN]] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.<ref>PMID:17177976</ref> <ref>PMID:18172500</ref> <ref>PMID:19344625</ref> <ref>PMID:19661379</ref>		[[http://www.uniprot.org/uniprot/PARP1_HUMAN PARP1_HUMAN]] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.<ref>PMID:17177976</ref> <ref>PMID:18172500</ref> <ref>PMID:19344625</ref> <ref>PMID:19661379</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Selective inhibitors could help unveil the mechanisms by which inhibition of poly(ADP-ribose) polymerases (PARPs) elicits clinical benefits in cancer therapy. We profiled 10 clinical PARP inhibitors and commonly used research tools for their inhibition of multiple PARP enzymes. We also determined crystal structures of these compounds bound to PARP1 or PARP2. Veliparib and niraparib are selective inhibitors of PARP1 and PARP2; olaparib, rucaparib, and talazoparib are more potent inhibitors of PARP1 but are less selective. PJ34 and UPF1069 are broad PARP inhibitors; PJ34 inserts a flexible moiety into hydrophobic subpockets in various ADP-ribosyltransferases. XAV939 is a promiscuous tankyrase inhibitor and a potent inhibitor of PARP1 in vitro and in cells, whereas IWR1 and AZ-6102 are tankyrase selective. Our biochemical and structural analysis of PARP inhibitor potencies establishes a molecular basis for either selectivity or promiscuity and provides a benchmark for experimental design in assessment of PARP inhibitor effects.
		+
		+	Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.,Thorsell AG, Ekblad T, Karlberg T, Low M, Pinto AF, Tresaugues L, Moche M, Cohen MS, Schuler H J Med Chem. 2016 Dec 21. PMID:28001384<ref>PMID:28001384</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4rv6" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Poly (ADP-ribose) polymerase\|Poly (ADP-ribose) polymerase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:10, 22 November 2017

OCA — Wed, 22 Nov 2017 09:10:40 GMT

←Older revision		Revision as of 09:10, 22 November 2017
Line 1:		Line 1:
		+
	==Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib==		==Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib==
	<StructureSection load='4rv6' size='340' side='right' caption='[[4rv6]], [[Resolution\|resolution]] 3.19Å' scene=''>		<StructureSection load='4rv6' size='340' side='right' caption='[[4rv6]], [[Resolution\|resolution]] 3.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rv6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RV6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4rv6]] is a 4 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=4RV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RV6 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RPB:RUCAPARIB'>RPB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RPB:RUCAPARIB'>RPB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4und\|4und]], [[4uxb\|4uxb]], [[4r5w\|4r5w]], [[4r6e\|4r6e]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4und\|4und]], [[4uxb\|4uxb]], [[4r5w\|4r5w]], [[4r6e\|4r6e]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADPRT, PARP1, PPOL ([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/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </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=4rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv6 OCA], [http://pdbe.org/4rv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rv6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rv6 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=4rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv6 OCA], [http://pdbe.org/4rv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rv6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Karlberg, T]]		[[Category: Karlberg, T]]
	[[Category: Schuler, H]]		[[Category: Schuler, H]]

OCA at 13:46, 9 December 2015

OCA — Wed, 09 Dec 2015 13:46:12 GMT

←Older revision		Revision as of 13:46, 9 December 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib==
-		+	<StructureSection load='4rv6' size='340' side='right' caption='[[4rv6]], [[Resolution\|resolution]] 3.19Å' scene=''>
-	~~The entry~~ 4rv6 is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4rv6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RV6 FirstGlance]. <br>
-	~~Authors~~: ~~Karlberg, T~~.~~, Thorsell, A~~.G.~~, Schuler, H~~.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RPB:RUCAPARIB'>RPB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4und\|4und]], [[4uxb\|4uxb]], [[4r5w\|4r5w]], [[4r6e\|4r6e]]</td></tr>
-	~~Description~~: ~~Human ARTD1~~ (~~PARP1~~) ~~catalytic domain in complex~~ with ~~inhibitor Rucaparib~~	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>
-	[~~[Category~~: ~~Unreleased Structures]~~]	+	<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=4rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv6 OCA], [http://pdbe.org/4rv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rv6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rv6 PDBsum]</span></td></tr>
-	[[~~Category~~: ~~Thorsell~~, A.G]]	+	</table>
-	[[~~Category~~: ~~Schuler, H~~]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PARP1_HUMAN PARP1_HUMAN]] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.<ref>PMID:17177976</ref> <ref>PMID:18172500</ref> <ref>PMID:19344625</ref> <ref>PMID:19661379</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Karlberg, T]]		[[Category: Karlberg, T]]
		+	[[Category: Schuler, H]]
		+	[[Category: Thorsell, A G]]
		+	[[Category: Adp-ribosyl transferase]]
		+	[[Category: Adp-ribosylation]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 12:09, 31 December 2014

OCA — Wed, 31 Dec 2014 12:09:58 GMT

←Older revision		Revision as of 12:09, 31 December 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4rv6 is ON HOLD	+	The entry 4rv6 is ON HOLD until Paper Publication

	Authors: Karlberg, T., Thorsell, A.G., Schuler, H.		Authors: Karlberg, T., Thorsell, A.G., Schuler, H.

OCA at 17:24, 24 December 2014

OCA — Wed, 24 Dec 2014 17:24:46 GMT

←Older revision		Revision as of 17:24, 24 December 2014
Line 6:		Line 6:

	Description: Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib		Description: Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib
		+	[[Category: Unreleased Structures]]
		+	[[Category: Thorsell, A.G]]
		+	[[Category: Schuler, H]]
		+	[[Category: Karlberg, T]]

OCA at 11:06, 17 December 2014

OCA — Wed, 17 Dec 2014 11:06:49 GMT

←Older revision		Revision as of 11:06, 17 December 2014
Line 5:		Line 5:
	Authors: Karlberg, T., Thorsell, A.G., Schuler, H.		Authors: Karlberg, T., Thorsell, A.G., Schuler, H.

-	Description: Human ARTD1 (PARP1) -catalytic domain in complex with inhibitor Rucaparib	+	Description: Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib

OCA: Protected "4rv6" [edit=sysop:move=sysop]

OCA — Wed, 03 Dec 2014 08:19:57 GMT

Protected "4rv6" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:19, 3 December 2014

OCA: New page: '''Unreleased structure''' The entry 4rv6 is ON HOLD Authors: Karlberg, T., Thorsell, A.G., Schuler, H. Description: Human ARTD1 (PARP1) -catalytic domain in complex with inhibitor Ruc...

OCA — Wed, 03 Dec 2014 08:19:56 GMT

New page: '''Unreleased structure''' The entry 4rv6 is ON HOLD Authors: Karlberg, T., Thorsell, A.G., Schuler, H. Description: Human ARTD1 (PARP1) -catalytic domain in complex with inhibitor Ruc...

New page

'''Unreleased structure'''

The entry 4rv6 is ON HOLD

Authors: Karlberg, T., Thorsell, A.G., Schuler, H.

Description: Human ARTD1 (PARP1) -catalytic domain in complex with inhibitor Rucaparib