7er1 - Revision history

OCA at 17:00, 29 November 2023

2023-11-29T17:00:26Z

←Older revision		Revision as of 17:00, 29 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7er1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_GI.3 Norovirus GI.3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[7er1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_GI.3 Norovirus GI.3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 03:47, 8 September 2022

2022-09-08T03:47:04Z

←Older revision		Revision as of 03:47, 8 September 2022
Line 1:		Line 1:

	==Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc==		==Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc==
-	<StructureSection load='7er1' size='340' side='right'caption='[[7er1]]' scene=''>	+	<StructureSection load='7er1' size='340' side='right'caption='[[7er1]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7er1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_GI.3 Norovirus GI.3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>
-	</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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human noroviruses (huNoVs) cause epidemic acute gastroenteritis using histo-blood group antigens (HBGAs) as host receptors or attachment factors to initiate an infection. While most huNoVs have been shown to bind HBGAs, some known clinical isolates, such as GI.3 DSV and VA115, do not recognize any HBGAs and thus the molecular mechanism behind their infections remains elusive. In this study, we provided both phenotypic and structural evidence to show that huNoV DSV and VA115 recognize a group of glycans with terminal galactoses as ligands. First, through glycan array we found that both DSV and VA115 protruding (P) domain proteins bound two oligosaccharides that share common terminal galactoses. Then, by determination of the crystal structures of DSV/VA115 P proteins in complex with Galalpha1-3Galbeta1-4Glc and/or NA2 N-Glycan, respectively, we showed that the terminal galactose is the main saccharide recognized by the two viral proteins. Our data demonstrated that GI huNoVs can interact with non-HBGA glycans through their conserved galactose binding site, shedding light on the mechanism of huNoV adaptation through recognizing new glycan receptors to facilitate their widespread nature in human population. These findings are also of significance in strategy development for huNoV control and prevention, as well as development of antiviral drugs. IMPORTANCE Human noroviruses (huNoVs) are the most important viral pathogens causing epidemic acute gastroenteritis worldwide. Previous studies indicated that histo-blood group antigens (HBGAs) are critical host-susceptibility factors affecting huNoV host susceptibility, host range, and probably prevalence. However, certain huNoVs, such as GI.3 DSV and VA115, do not recognize any HBGAs. This implies that other unknown host factors might exist and the molecular mechanism underlying their host receptor recognition or attachment remains elusive. In this study, we found that purified capsid protruding domain proteins from two GI.3 huNoVs specifically bind two glycans that contain a common terminal galactose. We solved the crystal structures of the complexes at atomic resolution and validated the vital amino acids involved in glycan recognition. Our findings elucidate the mechanism of GI.3 huNoV-non-HBGA glycan interaction, which explains why GI.3 virus strains could not bind human HBGAs, paving a way to the prevention and treatment of huNoV-associated diseases.
		+
		+	Structural Insight into Terminal Galactose Recognition by Two Non-HBGA Binding GI.3 Noroviruses.,Wang C, Kang H, Tan M, Cong J, Su D, Li X, Chen Y J Virol. 2022 Jun 6:e0042022. doi: 10.1128/jvi.00420-22. PMID:35658530<ref>PMID:35658530</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7er1" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Norovirus GI 3]]
	[[Category: Chen Y]]		[[Category: Chen Y]]

OCA at 14:30, 31 August 2022

2022-08-31T14:30:58Z

←Older revision		Revision as of 14:30, 31 August 2022
Line 1:		Line 1:

	==Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc==		==Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc==
-	<StructureSection load='7er1' size='340' side='right'caption='[[7er1]]~~, [[Resolution\|resolution]] 2.20Å~~' scene=''>	+	<StructureSection load='7er1' size='340' side='right'caption='[[7er1]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[7er1]] is a 4 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene></td></tr>	+	</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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 ProSAT]</span></td></tr>	+
	</table>		</table>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human noroviruses (huNoVs) cause epidemic acute gastroenteritis using histo-blood group antigens (HBGAs) as host receptors or attachment factors to initiate an infection. While most huNoVs have been shown to bind HBGAs, some known clinical isolates, such as GI.3 DSV and VA115, do not recognize any HBGAs and thus the molecular mechanism behind their infections remains elusive. In this study, we provided both phenotypic and structural evidence to show that huNoV DSV and VA115 recognize a group of glycans with terminal galactoses as ligands. First, through glycan array we found that both DSV and VA115 protruding (P) domain proteins bound two oligosaccharides that share common terminal galactoses. Then, by determination of the crystal structures of DSV/VA115 P proteins in complex with Galalpha1-3Galbeta1-4Glc and/or NA2 N-Glycan, respectively, we showed that the terminal galactose is the main saccharide recognized by the two viral proteins. Our data demonstrated that GI huNoVs can interact with non-HBGA glycans through their conserved galactose binding site, shedding light on the mechanism of huNoV adaptation through recognizing new glycan receptors to facilitate their widespread nature in human population. These findings are also of significance in strategy development for huNoV control and prevention, as well as development of antiviral drugs. IMPORTANCE Human noroviruses (huNoVs) are the most important viral pathogens causing epidemic acute gastroenteritis worldwide. Previous studies indicated that histo-blood group antigens (HBGAs) are critical host-susceptibility factors affecting huNoV host susceptibility, host range, and probably prevalence. However, certain huNoVs, such as GI.3 DSV and VA115, do not recognize any HBGAs. This implies that other unknown host factors might exist and the molecular mechanism underlying their host receptor recognition or attachment remains elusive. In this study, we found that purified capsid protruding domain proteins from two GI.3 huNoVs specifically bind two glycans that contain a common terminal galactose. We solved the crystal structures of the complexes at atomic resolution and validated the vital amino acids involved in glycan recognition. Our findings elucidate the mechanism of GI.3 huNoV-non-HBGA glycan interaction, which explains why GI.3 virus strains could not bind human HBGAs, paving a way to the prevention and treatment of huNoV-associated diseases.
-
-	Structural Insight into Terminal Galactose Recognition by Two Non-HBGA Binding GI.3 Noroviruses.,Wang C, Kang H, Tan M, Cong J, Su D, Li X, Chen Y J Virol. 2022 Jun 6:e0042022. doi: 10.1128/jvi.00420-22. PMID:35658530<ref>PMID:35658530</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 7er1" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chen, Y]]	+	[[Category: Chen Y]]
-	~~[[Category: Histo-blood group antigen]]~~	+
-	~~[[Category: Human norovirus]]~~	+
-	~~[[Category: Viral protein]]~~	+
-	~~[[Category: Viral receptor~~]]	+

OCA at 07:31, 29 June 2022

2022-06-29T07:31:23Z

←Older revision		Revision as of 07:31, 29 June 2022
Line 1:		Line 1:

	==Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc==		==Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc==
-	<StructureSection load='7er1' size='340' side='right'caption='[[7er1]]' scene=''>	+	<StructureSection load='7er1' size='340' side='right'caption='[[7er1]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7er1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>
-	</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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human noroviruses (huNoVs) cause epidemic acute gastroenteritis using histo-blood group antigens (HBGAs) as host receptors or attachment factors to initiate an infection. While most huNoVs have been shown to bind HBGAs, some known clinical isolates, such as GI.3 DSV and VA115, do not recognize any HBGAs and thus the molecular mechanism behind their infections remains elusive. In this study, we provided both phenotypic and structural evidence to show that huNoV DSV and VA115 recognize a group of glycans with terminal galactoses as ligands. First, through glycan array we found that both DSV and VA115 protruding (P) domain proteins bound two oligosaccharides that share common terminal galactoses. Then, by determination of the crystal structures of DSV/VA115 P proteins in complex with Galalpha1-3Galbeta1-4Glc and/or NA2 N-Glycan, respectively, we showed that the terminal galactose is the main saccharide recognized by the two viral proteins. Our data demonstrated that GI huNoVs can interact with non-HBGA glycans through their conserved galactose binding site, shedding light on the mechanism of huNoV adaptation through recognizing new glycan receptors to facilitate their widespread nature in human population. These findings are also of significance in strategy development for huNoV control and prevention, as well as development of antiviral drugs. IMPORTANCE Human noroviruses (huNoVs) are the most important viral pathogens causing epidemic acute gastroenteritis worldwide. Previous studies indicated that histo-blood group antigens (HBGAs) are critical host-susceptibility factors affecting huNoV host susceptibility, host range, and probably prevalence. However, certain huNoVs, such as GI.3 DSV and VA115, do not recognize any HBGAs. This implies that other unknown host factors might exist and the molecular mechanism underlying their host receptor recognition or attachment remains elusive. In this study, we found that purified capsid protruding domain proteins from two GI.3 huNoVs specifically bind two glycans that contain a common terminal galactose. We solved the crystal structures of the complexes at atomic resolution and validated the vital amino acids involved in glycan recognition. Our findings elucidate the mechanism of GI.3 huNoV-non-HBGA glycan interaction, which explains why GI.3 virus strains could not bind human HBGAs, paving a way to the prevention and treatment of huNoV-associated diseases.
		+
		+	Structural Insight into Terminal Galactose Recognition by Two Non-HBGA Binding GI.3 Noroviruses.,Wang C, Kang H, Tan M, Cong J, Su D, Li X, Chen Y J Virol. 2022 Jun 6:e0042022. doi: 10.1128/jvi.00420-22. PMID:35658530<ref>PMID:35658530</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7er1" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chen Y]]	+	[[Category: Chen, Y]]
		+	[[Category: Histo-blood group antigen]]
		+	[[Category: Human norovirus]]
		+	[[Category: Viral protein]]
		+	[[Category: Viral receptor]]

OCA at 06:17, 12 May 2022

2022-05-12T06:17:03Z

←Older revision		Revision as of 06:17, 12 May 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 7er1 is ON HOLD until Paper Publication~~	+	==Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc==
-		+	<StructureSection load='7er1' size='340' side='right'caption='[[7er1]]' scene=''>
-	~~Authors: Chen, Y.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ER1 FirstGlance]. <br>
-	~~Description:~~ Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc	+	</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=7er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7er1 OCA], [https://pdbe.org/7er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7er1 RCSB], [https://www.ebi.ac.uk/pdbsum/7er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7er1 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Chen, Y]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Chen Y]]

OCA at 10:19, 27 April 2022

2022-04-27T10:19:34Z

←Older revision		Revision as of 10:19, 27 April 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7er1 is ON HOLD	+	The entry 7er1 is ON HOLD until Paper Publication

	Authors: Chen, Y.		Authors: Chen, Y.

OCA at 08:42, 19 May 2021

2021-05-19T08:42:23Z

←Older revision		Revision as of 08:42, 19 May 2021
Line 3:		Line 3:
	The entry 7er1 is ON HOLD		The entry 7er1 is ON HOLD

-	Authors: ~~Yutao~~, C.	+	Authors: Chen, Y.

	Description: Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc		Description: Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Yutao~~, C]]	+	[[Category: Chen, Y]]

OCA: Protected "7er1" [edit=sysop:move=sysop]

2021-05-12T08:05:21Z

Protected "7er1" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:05, 12 May 2021

OCA: New page: '''Unreleased structure''' The entry 7er1 is ON HOLD Authors: Yutao, C. Description: Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc [[Cat...

2021-05-12T08:05:20Z

New page: '''Unreleased structure''' The entry 7er1 is ON HOLD Authors: Yutao, C. Description: Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc [[Cat...

New page

'''Unreleased structure'''

The entry 7er1 is ON HOLD

Authors: Yutao, C.

Description: Crystal structure of capsid P domain of norovirus GI.3 VA115 complexed with Gala1-3Galb1-4Glc
[[Category: Unreleased Structures]]
[[Category: Yutao, C]]