4x52 - Revision history

OCA at 10:47, 10 January 2024

OCA — Wed, 10 Jan 2024 10:47:12 GMT

←Older revision		Revision as of 10:47, 10 January 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4x52]] 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=4X52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X52 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4x52]] 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=4X52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X52 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.08Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [https://pdbe.org/4x52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [https://www.ebi.ac.uk/pdbsum/4x52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x52 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=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [https://pdbe.org/4x52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [https://www.ebi.ac.uk/pdbsum/4x52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x52 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 21:12, 12 April 2023

OCA — Wed, 12 Apr 2023 21:12:57 GMT

←Older revision		Revision as of 21:12, 12 April 2023
Line 1:		Line 1:

	==Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)==		==Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)==
-	<StructureSection load='4x52' size='340' side='right' caption='[[4x52]], [[Resolution\|resolution]] 2.08Å' scene=''>	+	<StructureSection load='4x52' size='340' side='right'caption='[[4x52]], [[Resolution\|resolution]] 2.08Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4x52]] 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=4X52 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4X52 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4x52]] 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=4X52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X52 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=GOL:GLYCEROL'>GOL</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">[[2x5y\|2x5y]]</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=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [https://pdbe.org/4x52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [https://www.ebi.ac.uk/pdbsum/4x52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x52 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ZC3HAV1, ZC3HDC2, PRO1677 ([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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [~~http~~://pdbe.org/4x52 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4x52 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4x52 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ZCCHV_HUMAN ZCCHV_HUMAN]] Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs).<ref>PMID:18225958</ref> <ref>PMID:21102435</ref> <ref>PMID:21876179</ref> <ref>PMID:22720057</ref>	+	[https://www.uniprot.org/uniprot/ZCCHV_HUMAN ZCCHV_HUMAN] Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs).<ref>PMID:18225958</ref> <ref>PMID:21102435</ref> <ref>PMID:21876179</ref> <ref>PMID:22720057</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: Karlberg, T]]	+	[[Category: Large Structures]]
-	[[Category: Klepsch, M]]	+	[[Category: Karlberg T]]
-	[[Category: Schuler, H]]	+	[[Category: Klepsch M]]
-	[[Category: Thorsell~~, A G]]~~	+	[[Category: Schuler H]]
-	~~[[Category: Antiviral defense]]~~	+	[[Category: Thorsell AG]]
-	~~[[Category: Immune system]]~~	+
-	~~[[Category: Mutant]]~~	+
-	~~[[Category: Parp]]~~	+
-	~~[[Category: Zap~~]]	+

OCA at 07:56, 17 January 2018

OCA — Wed, 17 Jan 2018 07:56:53 GMT

←Older revision		Revision as of 07:56, 17 January 2018
Line 3:		Line 3:
	<StructureSection load='4x52' size='340' side='right' caption='[[4x52]], [[Resolution\|resolution]] 2.08Å' scene=''>		<StructureSection load='4x52' size='340' side='right' caption='[[4x52]], [[Resolution\|resolution]] 2.08Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4x52]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X52 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4x52]] 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=4X52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X52 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=GOL:GLYCEROL'>GOL</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">[[2x5y\|2x5y]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5y\|2x5y]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ZC3HAV1, ZC3HDC2, PRO1677 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [http://pdbe.org/4x52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [http://www.ebi.ac.uk/pdbsum/4x52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x52 ProSAT]</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=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [http://pdbe.org/4x52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [http://www.ebi.ac.uk/pdbsum/4x52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x52 ProSAT]</span></td></tr>
	</table>		</table>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Karlberg, T]]		[[Category: Karlberg, T]]
	[[Category: Klepsch, M]]		[[Category: Klepsch, M]]

OCA at 00:24, 26 January 2017

OCA — Thu, 26 Jan 2017 00:24:10 GMT

←Older revision		Revision as of 00:24, 26 January 2017
Line 1:		Line 1:
		+
	==Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)==		==Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)==
	<StructureSection load='4x52' size='340' side='right' caption='[[4x52]], [[Resolution\|resolution]] 2.08Å' scene=''>		<StructureSection load='4x52' size='340' side='right' caption='[[4x52]], [[Resolution\|resolution]] 2.08Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=GOL:GLYCEROL'>GOL</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">[[2x5y\|2x5y]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5y\|2x5y]]</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=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [http://www.ebi.ac.uk/pdbsum/4x52 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=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [http://pdbe.org/4x52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [http://www.ebi.ac.uk/pdbsum/4x52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x52 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4x52" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:51, 12 February 2015

OCA — Thu, 12 Feb 2015 11:51:39 GMT

←Older revision		Revision as of 11:51, 12 February 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)==
		+	<StructureSection load='4x52' size='340' side='right' caption='[[4x52]], [[Resolution\|resolution]] 2.08Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4x52]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X52 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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">[[2x5y\|2x5y]]</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=4x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x52 RCSB], [http://www.ebi.ac.uk/pdbsum/4x52 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ZCCHV_HUMAN ZCCHV_HUMAN]] Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs).<ref>PMID:18225958</ref> <ref>PMID:21102435</ref> <ref>PMID:21876179</ref> <ref>PMID:22720057</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The mammalian poly(ADP-ribose) polymerase (PARP) family are ADP-ribosyltransferases with diphtheria toxin homology (ARTD). Most members have mono-ADP-ribosyltransferase activity. PARP13/ARTD13, also called zinc finger antiviral protein (ZAP), has roles in viral immunity and microRNA mediated stress responses. PARP13 features a divergent PARP homology domain missing a PARP consensus sequence motif; the domain has enigmatic functions and apparently lacks catalytic activity. We used X-ray crystallography, molecular dynamics simulations and biochemical analyses to investigate the structural requirements for ADP-ribosyltransferase activity in human PARP13 and two of its functional partners in stress granules, PARP12/ARTD12, and PARP15/ BAL3/ARTD7. The crystal structure of the PARP homology domain of PARP13 shows obstruction of the canonical active site, precluding NAD+ binding. Molecular dynamics simulations indicate that this closed cleft conformation is maintained in solution. Introducing consensus side chains in PARP13 did not result in 3-aminobenzamide binding, but in further closure of the site. Three-dimensional alignment of the PARP homology domains of PARP13, PARP12, and PARP15 illustrates placement of PARP13 residues that deviate from the PARP family consensus. Introducing either one of two of these side chains into the corresponding positions in PARP15 abolished PARP15 ADP-ribosyltransferase activity. Taken together, our results show that PARP13 lacks the structural requirements for ADP-ribosyltransferase activity.

-	~~The entry 4x52 is ON HOLD until Paper Publication~~	+	Structural Basis for Lack of ADP-Ribosyltransferase Activity in Poly(ADP-Ribose) Polymerase-13/Zinc Finger Antiviral Protein.,Karlberg T, Klepsch M, Thorsell AG, Andersson CD, Linusson A, Schuler H J Biol Chem. 2015 Jan 29. pii: jbc.M114.630160. PMID:25635049<ref>PMID:25635049</ref>

-	~~Authors: Karlberg~~, T.~~, Thorsell, A~~.~~G., Klepsch, M., Schuler, H~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
-	~~[[Category: Thorsell, A.G]]~~	+	__TOC__
		+	</StructureSection>
	[[Category: Karlberg, T]]		[[Category: Karlberg, T]]
	[[Category: Klepsch, M]]		[[Category: Klepsch, M]]
	[[Category: Schuler, H]]		[[Category: Schuler, H]]
		+	[[Category: Thorsell, A G]]
		+	[[Category: Antiviral defense]]
		+	[[Category: Immune system]]
		+	[[Category: Mutant]]
		+	[[Category: Parp]]
		+	[[Category: Zap]]

OCA at 20:29, 24 December 2014

OCA — Wed, 24 Dec 2014 20:29:58 GMT

←Older revision		Revision as of 20:29, 24 December 2014
Line 6:		Line 6:

	Description: Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)		Description: Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)
		+	[[Category: Unreleased Structures]]
		+	[[Category: Thorsell, A.G]]
		+	[[Category: Karlberg, T]]
		+	[[Category: Klepsch, M]]
		+	[[Category: Schuler, H]]

OCA at 11:41, 17 December 2014

OCA — Wed, 17 Dec 2014 11:41:52 GMT

←Older revision		Revision as of 11:41, 17 December 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4x52 is ON HOLD	+	The entry 4x52 is ON HOLD until Paper Publication

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

	Description: Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)		Description: Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)

OCA: Protected "4x52" [edit=sysop:move=sysop]

OCA — Wed, 10 Dec 2014 14:23:24 GMT

Protected "4x52" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:23, 10 December 2014

OCA: New page: '''Unreleased structure''' The entry 4x52 is ON HOLD Authors: Karlberg, T., Thorsell, A.G., Klepsch, M., Schuler, H. Description: Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N;...

OCA — Wed, 10 Dec 2014 14:23:22 GMT

New page: '''Unreleased structure''' The entry 4x52 is ON HOLD Authors: Karlberg, T., Thorsell, A.G., Klepsch, M., Schuler, H. Description: Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N;...

New page

'''Unreleased structure'''

The entry 4x52 is ON HOLD

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

Description: Human PARP13 (ZC3HAV1), C-Terminal PARP Domain (H810N; N830Y variant)