5dus - Revision history

OCA at 09:10, 20 March 2024

OCA — Wed, 20 Mar 2024 09:10:24 GMT

←Older revision		Revision as of 09:10, 20 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/R1A_MERS1 R1A_MERS1] The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.[UniProtKB:P0C6X7] Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.<ref>PMID:26311885</ref> May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling.[UniProtKB:P0C6X7]<ref>PMID:25142582</ref> Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7][PROSITE-ProRule:PRU00772] Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7]		[https://www.uniprot.org/uniprot/R1A_MERS1 R1A_MERS1] The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.[UniProtKB:P0C6X7] Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.<ref>PMID:26311885</ref> May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling.[UniProtKB:P0C6X7]<ref>PMID:25142582</ref> Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7][PROSITE-ProRule:PRU00772] Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV) encodes the conserved macro domain within non-structural protein 3. However, the precise biochemical function and structure of the macro domain is unclear. Using differential scanning fluorimetry and isothermal titration calorimetry, we characterized the MERS-CoV macro domain as a more efficient adenosine diphosphate (ADP)-ribose binding module than macro domains from other CoVs. Furthermore, the crystal structure of the MERS-CoV macro domain was determined at 1.43-A resolution in complex with ADP-ribose. Comparison of macro domains from MERS-CoV and other human CoVs revealed structural differences in the alpha1 helix alters how the conserved Asp-20 interacts with ADP-ribose and may explain the efficient binding of the MERS-CoV macro domain to ADP-ribose. This study provides structural and biophysical bases to further evaluate the role of the MERS-CoV macro domain in the host response via ADP-ribose binding but also as a potential target for drug design.
-
-	Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES.,Cho CC, Lin MH, Chuang CY, Hsu CH J Biol Chem. 2016 Mar 4;291(10):4894-902. doi: 10.1074/jbc.M115.700542. Epub 2016, Jan 5. PMID:26740631<ref>PMID:26740631</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5dus" style="background-color:#fffaf0;"></div>

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

OCA at 22:01, 28 June 2023

OCA — Wed, 28 Jun 2023 22:01:00 GMT

←Older revision		Revision as of 22:01, 28 June 2023
Line 3:		Line 3:
	<StructureSection load='5dus' size='340' side='right'caption='[[5dus]], [[Resolution\|resolution]] 1.43Å' scene=''>		<StructureSection load='5dus' size='340' side='right'caption='[[5dus]], [[Resolution\|resolution]] 1.43Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5dus]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Mers Mers~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5DUS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5dus]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Middle_East_respiratory_syndrome-related_coronavirus Middle East respiratory syndrome-related coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DUS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <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]] 1.432Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [~~http~~://pdbe.org/5dus PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5dus PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5dus ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <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=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [https://pdbe.org/5dus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [https://www.ebi.ac.uk/pdbsum/5dus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dus ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/R1A_MERS1 R1A_MERS1] The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.[UniProtKB:P0C6X7] Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.<ref>PMID:26311885</ref> May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling.[UniProtKB:P0C6X7]<ref>PMID:25142582</ref> Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7][PROSITE-ProRule:PRU00772] Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 16:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5dus" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5dus" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Virus protease 3D structures\|Virus protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 21:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Mers~~]]	+	[[Category: Middle East respiratory syndrome-related coronavirus]]
-	[[Category: Cho, C C]]	+	[[Category: Cho C-C]]
-	[[Category: Chuang, C Y]]	+	[[Category: Chuang C-Y]]
-	[[Category: Hsu, C H]]	+	[[Category: Hsu C-H]]
-	[[Category: Lin, M H]]	+	[[Category: Lin M-H]]
-	~~[[Category: Adp-ribose]]~~	+
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Ligand]]~~	+
-	~~[[Category: Macro domain]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 08:07, 15 April 2020

OCA — Wed, 15 Apr 2020 08:07:27 GMT

←Older revision		Revision as of 08:07, 15 April 2020
Line 1:		Line 1:

	==Crystal structure of MERS-CoV macro domain in complex with ADP-ribose==		==Crystal structure of MERS-CoV macro domain in complex with ADP-ribose==
-	<StructureSection load='5dus' size='340' side='right' caption='[[5dus]], [[Resolution\|resolution]] 1.43Å' scene=''>	+	<StructureSection load='5dus' size='340' side='right'caption='[[5dus]], [[Resolution\|resolution]] 1.43Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5dus]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUS OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5DUS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5dus]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mers Mers]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DUS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <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=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <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'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [http://pdbe.org/5dus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [http://www.ebi.ac.uk/pdbsum/5dus PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [http://pdbe.org/5dus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [http://www.ebi.ac.uk/pdbsum/5dus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dus ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 20:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Mers]]
	[[Category: Cho, C C]]		[[Category: Cho, C C]]
	[[Category: Chuang, C Y]]		[[Category: Chuang, C Y]]

OCA at 18:51, 10 May 2016

OCA — Tue, 10 May 2016 18:51:45 GMT

←Older revision		Revision as of 18:51, 10 May 2016
Line 1:		Line 1:
		+
	==Crystal structure of MERS-CoV macro domain in complex with ADP-ribose==		==Crystal structure of MERS-CoV macro domain in complex with ADP-ribose==
	<StructureSection load='5dus' size='340' side='right' caption='[[5dus]], [[Resolution\|resolution]] 1.43Å' scene=''>		<StructureSection load='5dus' size='340' side='right' caption='[[5dus]], [[Resolution\|resolution]] 1.43Å' scene=''>
Line 6:		Line 7:
	<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=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [http://pdbe.org/5dus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [http://www.ebi.ac.uk/pdbsum/5dus 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=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [http://pdbe.org/5dus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [http://www.ebi.ac.uk/pdbsum/5dus PDBsum]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV) encodes the conserved macro domain within non-structural protein 3. However, the precise biochemical function and structure of the macro domain is unclear. Using differential scanning fluorimetry and isothermal titration calorimetry, we characterized the MERS-CoV macro domain as a more efficient adenosine diphosphate (ADP)-ribose binding module than macro domains from other CoVs. Furthermore, the crystal structure of the MERS-CoV macro domain was determined at 1.43-A resolution in complex with ADP-ribose. Comparison of macro domains from MERS-CoV and other human CoVs revealed structural differences in the alpha1 helix alters how the conserved Asp-20 interacts with ADP-ribose and may explain the efficient binding of the MERS-CoV macro domain to ADP-ribose. This study provides structural and biophysical bases to further evaluate the role of the MERS-CoV macro domain in the host response via ADP-ribose binding but also as a potential target for drug design.
		+
		+	Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES.,Cho CC, Lin MH, Chuang CY, Hsu CH J Biol Chem. 2016 Mar 4;291(10):4894-902. doi: 10.1074/jbc.M115.700542. Epub 2016, Jan 5. PMID:26740631<ref>PMID:26740631</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5dus" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 20:32, 13 January 2016

OCA — Wed, 13 Jan 2016 20:32:18 GMT

←Older revision		Revision as of 20:32, 13 January 2016
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of MERS-CoV macro domain in complex with ADP-ribose==
-		+	<StructureSection load='5dus' size='340' side='right' caption='[[5dus]], [[Resolution\|resolution]] 1.43Å' scene=''>
-	~~The entry~~ 5dus is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5dus]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DUS FirstGlance]. <br>
-	~~Authors~~: ~~Cho, C~~.-C.~~, Lin, M~~.-H.~~, Chuang, C~~.-Y.~~, Hsu, C~~.-H.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [http://pdbe.org/5dus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [http://www.ebi.ac.uk/pdbsum/5dus PDBsum]</span></td></tr>
-	~~Description~~: ~~Crystal structure of MERS~~-~~CoV macro domain in complex with ADP~~-~~ribose~~	+	</table>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	__TOC__
-	[[Category: ~~Hsu~~, C~~.-H~~]]	+	</StructureSection>
-	[[Category: Chuang, C.-Y]]	+	[[Category: Cho, C C]]
-	[[Category: ~~Cho~~, C~~.-C~~]]	+	[[Category: Chuang, C Y]]
-	[[Category: Lin, M.-H]]	+	[[Category: Hsu, C H]]
		+	[[Category: Lin, M H]]
		+	[[Category: Adp-ribose]]
		+	[[Category: Complex]]
		+	[[Category: Ligand]]
		+	[[Category: Macro domain]]
		+	[[Category: Viral protein]]

OCA at 11:26, 16 December 2015

OCA — Wed, 16 Dec 2015 11:26:14 GMT

←Older revision		Revision as of 11:26, 16 December 2015
Line 7:		Line 7:
	Description: Crystal structure of MERS-CoV macro domain in complex with ADP-ribose		Description: Crystal structure of MERS-CoV macro domain in complex with ADP-ribose
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Hsu, C.-H]]
	[[Category: Chuang, C.-Y]]		[[Category: Chuang, C.-Y]]
	[[Category: Cho, C.-C]]		[[Category: Cho, C.-C]]
-	[[Category: Hsu, C.-H]]
	[[Category: Lin, M.-H]]		[[Category: Lin, M.-H]]

OCA at 02:11, 1 December 2015

OCA — Tue, 01 Dec 2015 02:11:40 GMT

←Older revision		Revision as of 02:11, 1 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5dus is ON HOLD	+	The entry 5dus is ON HOLD until Paper Publication

	Authors: Cho, C.-C., Lin, M.-H., Chuang, C.-Y., Hsu, C.-H.		Authors: Cho, C.-C., Lin, M.-H., Chuang, C.-Y., Hsu, C.-H.

OCA: Protected "5dus" [edit=sysop:move=sysop]

OCA — Wed, 30 Sep 2015 13:33:33 GMT

Protected "5dus" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:33, 30 September 2015

OCA: New page: '''Unreleased structure''' The entry 5dus is ON HOLD Authors: Cho, C.-C., Lin, M.-H., Chuang, C.-Y., Hsu, C.-H. Description: Crystal structure of MERS-CoV macro domain in complex with ...

OCA — Wed, 30 Sep 2015 13:33:32 GMT

New page: '''Unreleased structure''' The entry 5dus is ON HOLD Authors: Cho, C.-C., Lin, M.-H., Chuang, C.-Y., Hsu, C.-H. Description: Crystal structure of MERS-CoV macro domain in complex with ...

New page

'''Unreleased structure'''

The entry 5dus is ON HOLD

Authors: Cho, C.-C., Lin, M.-H., Chuang, C.-Y., Hsu, C.-H.

Description: Crystal structure of MERS-CoV macro domain in complex with ADP-ribose
[[Category: Unreleased Structures]]
[[Category: Chuang, C.-Y]]
[[Category: Cho, C.-C]]
[[Category: Hsu, C.-H]]
[[Category: Lin, M.-H]]