5zuv - Revision history

OCA at 09:08, 22 November 2023

OCA — Wed, 22 Nov 2023 09:08:17 GMT

←Older revision		Revision as of 09:08, 22 November 2023
Line 3:		Line 3:
	<StructureSection load='5zuv' size='340' side='right'caption='[[5zuv]], [[Resolution\|resolution]] 2.21Å' scene=''>		<StructureSection load='5zuv' size='340' side='right'caption='[[5zuv]], [[Resolution\|resolution]] 2.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zuv]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Cvh22 Cvh22~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ZUV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zuv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_coronavirus_229E Human coronavirus 229E] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZUV FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.21Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~S, 2 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11137 CVH22])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5zuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zuv OCA], [~~http~~://pdbe.org/5zuv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5zuv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5zuv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5zuv 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=5zuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zuv OCA], [https://pdbe.org/5zuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zuv RCSB], [https://www.ebi.ac.uk/pdbsum/5zuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zuv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SPIKE_CVH22 SPIKE_CVH22]] S1 region attaches the virion to the cell membrane by interacting with human ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes (By similarity).	+	[https://www.uniprot.org/uniprot/SPIKE_CVH22 SPIKE_CVH22] S1 region attaches the virion to the cell membrane by interacting with human ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5zuv" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5zuv" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Sandbox 3001\|Sandbox 3001]]
		+	*[[Spike protein\|Spike protein]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cvh22~~]]	+	[[Category: Human coronavirus 229E]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Wilson, I A~~]]	+	[[Category: Synthetic construct]]
-	[[Category: ~~Yan, L~~]]	+	[[Category: Wilson IA]]
-	[[Category: ~~Yang, B~~]]	+	[[Category: Yan L]]
-	[[Category: ~~Hr1 motif]]~~	+	[[Category: Yang B]]
-	~~[[Category: Human coronavirus 229e]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Pan-coronavirus]]~~	+
-	~~[[Category: S2 domain]]~~	+
-	~~[[Category: Spike protein]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 08:07, 21 May 2019

OCA — Tue, 21 May 2019 08:07:58 GMT

←Older revision		Revision as of 08:07, 21 May 2019
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SPIKE_CVH22 SPIKE_CVH22]] S1 region attaches the virion to the cell membrane by interacting with human ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes (By similarity).		[[http://www.uniprot.org/uniprot/SPIKE_CVH22 SPIKE_CVH22]] S1 region attaches the virion to the cell membrane by interacting with human ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Continuously emerging highly pathogenic human coronaviruses (HCoVs) remain a major threat to human health, as illustrated in past SARS-CoV and MERS-CoV outbreaks. The development of a drug with broad-spectrum HCoV inhibitory activity would address this urgent unmet medical need. Although previous studies have suggested that the HR1 of HCoV spike (S) protein is an important target site for inhibition against specific HCoVs, whether this conserved region could serve as a target for the development of broad-spectrum pan-CoV inhibitor remains controversial. Here, we found that peptide OC43-HR2P, derived from the HR2 domain of HCoV-OC43, exhibited broad fusion inhibitory activity against multiple HCoVs. EK1, the optimized form of OC43-HR2P, showed substantially improved pan-CoV fusion inhibitory activity and pharmaceutical properties. Crystal structures indicated that EK1 can form a stable six-helix bundle structure with both short alpha-HCoV and long beta-HCoV HR1s, further supporting the role of HR1 region as a viable pan-CoV target site.
		+
		+	A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike.,Xia S, Yan L, Xu W, Agrawal AS, Algaissi A, Tseng CK, Wang Q, Du L, Tan W, Wilson IA, Jiang S, Yang B, Lu L Sci Adv. 2019 Apr 10;5(4):eaav4580. doi: 10.1126/sciadv.aav4580. eCollection 2019, Apr. PMID:30989115<ref>PMID:30989115</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5zuv" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:34, 17 April 2019

OCA — Wed, 17 Apr 2019 06:34:12 GMT

←Older revision		Revision as of 06:34, 17 April 2019
Line 3:		Line 3:
	<StructureSection load='5zuv' size='340' side='right'caption='[[5zuv]], [[Resolution\|resolution]] 2.21Å' scene=''>		<StructureSection load='5zuv' size='340' side='right'caption='[[5zuv]], [[Resolution\|resolution]] 2.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zuv]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZUV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zuv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvh22 Cvh22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZUV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S, 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11137 CVH22])</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=5zuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zuv OCA], [http://pdbe.org/5zuv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zuv RCSB], [http://www.ebi.ac.uk/pdbsum/5zuv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zuv 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=5zuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zuv OCA], [http://pdbe.org/5zuv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zuv RCSB], [http://www.ebi.ac.uk/pdbsum/5zuv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zuv ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Cvh22]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Wilson, I A]]		[[Category: Wilson, I A]]

OCA at 07:06, 10 April 2019

OCA — Wed, 10 Apr 2019 07:06:21 GMT

←Older revision		Revision as of 07:06, 10 April 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5zuv is ~~ON HOLD until Paper Publication~~	+	==Crystal Structure of the Human Coronavirus 229E HR1 motif in complex with pan-CoVs inhibitor EK1==
-		+	<StructureSection load='5zuv' size='340' side='right'caption='[[5zuv]], [[Resolution\|resolution]] 2.21Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5zuv]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZUV FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5zuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zuv OCA], [http://pdbe.org/5zuv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zuv RCSB], [http://www.ebi.ac.uk/pdbsum/5zuv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zuv ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SPIKE_CVH22 SPIKE_CVH22]] S1 region attaches the virion to the cell membrane by interacting with human ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes (By similarity).
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Wilson, I A]]
		+	[[Category: Yan, L]]
		+	[[Category: Yang, B]]
		+	[[Category: Hr1 motif]]
		+	[[Category: Human coronavirus 229e]]
		+	[[Category: Inhibitor]]
		+	[[Category: Pan-coronavirus]]
		+	[[Category: S2 domain]]
		+	[[Category: Spike protein]]
		+	[[Category: Viral protein]]

OCA at 03:51, 30 May 2018

OCA — Wed, 30 May 2018 03:51:45 GMT

←Older revision		Revision as of 03:51, 30 May 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Wed, 16 May 2018 03:54:45 GMT

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

←Older revision

Revision as of 03:54, 16 May 2018

OCA: New page: '''Unreleased structure''' The entry 5zuv is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 16 May 2018 03:54:44 GMT

New page: '''Unreleased structure''' The entry 5zuv is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5zuv is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]