4q0x - Revision history

OCA at 07:39, 8 February 2023

2023-02-08T07:39:46Z

←Older revision		Revision as of 07:39, 8 February 2023
Line 3:		Line 3:
	<StructureSection load='4q0x' size='340' side='right'caption='[[4q0x]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4q0x' size='340' side='right'caption='[[4q0x]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Hepatitis_c_virus Hepatitis c virus~~] and [~~http~~://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepacivirus_C Hepacivirus C] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hzl\|4hzl]]</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=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [https://pdbe.org/4q0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [https://www.ebi.ac.uk/pdbsum/4q0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0x 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=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [~~http~~://pdbe.org/4q0x PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4q0x PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0x ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~POLG_HCVH POLG_HCVH~~]] Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).<ref>PMID:16894197</ref> E1 and E2 glycoproteins form a heterodimer that is involved in virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to human LDLR, CD81 and SCARB1/SR-BI receptors, but this binding is not sufficient for infection, some additional liver specific cofactors may be needed. The fusion function may possibly be carried by E1. E2 inhibits human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses. These interactions allow capture of circulating HCV particles by these cells and subsequent transmission to permissive cells. DCs act as sentinels in various tissues where they entrap pathogens and convey them to local lymphoid tissue or lymph node for establishment of immunity. Capture of circulating HCV particles by these SIGN+ cells may facilitate virus infection of proximal hepatocytes and lymphocyte subpopulations and may be essential for the establishment of persistent infection (By similarity).<ref>PMID:16894197</ref> P7 seems to be a heptameric ion channel protein (viroporin) and is inhibited by the antiviral drug amantadine (By similarity). Also inhibited by long-alkyl-chain iminosugar derivatives. Essential for infectivity.<ref>PMID:16894197</ref> Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation (By similarity).<ref>PMID:16894197</ref> NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand (By similarity). Cleaves and inhibits the host antiviral protein MAVS.<ref>PMID:16894197</ref> NS4B induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex. NS4B polymerization or in protein-protein interactions activity may contribute to its function in membranous web formation.<ref>PMID:16894197</ref> NS5A is a component of the replication complex involved in RNA-binding. Its interaction with Human VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation. Mediates interferon resistance, presumably by interacting with and inhibiting human EIF2AK2/PKR. Seems to inhibit apoptosis by interacting with BIN1 and FKBP8. The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity).<ref>PMID:16894197</ref> NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication.<ref>PMID:16894197</ref>	+	[https://www.uniprot.org/uniprot/Q99LC4_MOUSE Q99LC4_MOUSE]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 4q0x" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4q0x" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Monoclonal Antibodies 3D structures\|Monoclonal Antibodies 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Hepatitis c virus~~]]	+	[[Category: Hepacivirus C]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Deng, L]]	+	[[Category: Deng L]]
-	[[Category: Zhang, P]]	+	[[Category: Zhang P]]
-	~~[[Category: Anti-hcv e2]]~~	+
-	~~[[Category: Antibody]]~~	+
-	~~[[Category: Hcv e2]]~~	+
-	~~[[Category: Immune system-viral protein complex~~]]	+

OCA at 08:21, 17 April 2019

2019-04-17T08:21:01Z

←Older revision		Revision as of 08:21, 17 April 2019
Line 1:		Line 1:

	==Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2==		==Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2==
-	<StructureSection load='4q0x' size='340' side='right' caption='[[4q0x]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='4q0x' size='340' side='right'caption='[[4q0x]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>		<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Hepatitis c virus]]		[[Category: Hepatitis c virus]]
		+	[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Deng, L]]		[[Category: Deng, L]]

OCA at 15:37, 5 August 2016

2016-08-05T15:37:25Z

←Older revision		Revision as of 15:37, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2==		==Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2==
	<StructureSection load='4q0x' size='340' side='right' caption='[[4q0x]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4q0x' size='340' side='right' caption='[[4q0x]], [[Resolution\|resolution]] 2.90Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>		<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hzl\|4hzl]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hzl\|4hzl]]</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=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [http://www.ebi.ac.uk/pdbsum/4q0x 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=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [http://pdbe.org/4q0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [http://www.ebi.ac.uk/pdbsum/4q0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4q0x" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:58, 25 December 2014

2014-12-25T19:58:03Z

←Older revision		Revision as of 19:58, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>		<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hzl\|4hzl]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hzl\|4hzl]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [http://www.ebi.ac.uk/pdbsum/4q0x 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=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [http://www.ebi.ac.uk/pdbsum/4q0x PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLG_HCVH POLG_HCVH]] Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).<ref>PMID:16894197</ref> E1 and E2 glycoproteins form a heterodimer that is involved in virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to human LDLR, CD81 and SCARB1/SR-BI receptors, but this binding is not sufficient for infection, some additional liver specific cofactors may be needed. The fusion function may possibly be carried by E1. E2 inhibits human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses. These interactions allow capture of circulating HCV particles by these cells and subsequent transmission to permissive cells. DCs act as sentinels in various tissues where they entrap pathogens and convey them to local lymphoid tissue or lymph node for establishment of immunity. Capture of circulating HCV particles by these SIGN+ cells may facilitate virus infection of proximal hepatocytes and lymphocyte subpopulations and may be essential for the establishment of persistent infection (By similarity).<ref>PMID:16894197</ref> P7 seems to be a heptameric ion channel protein (viroporin) and is inhibited by the antiviral drug amantadine (By similarity). Also inhibited by long-alkyl-chain iminosugar derivatives. Essential for infectivity.<ref>PMID:16894197</ref> Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation (By similarity).<ref>PMID:16894197</ref> NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand (By similarity). Cleaves and inhibits the host antiviral protein MAVS.<ref>PMID:16894197</ref> NS4B induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex. NS4B polymerization or in protein-protein interactions activity may contribute to its function in membranous web formation.<ref>PMID:16894197</ref> NS5A is a component of the replication complex involved in RNA-binding. Its interaction with Human VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation. Mediates interferon resistance, presumably by interacting with and inhibiting human EIF2AK2/PKR. Seems to inhibit apoptosis by interacting with BIN1 and FKBP8. The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity).<ref>PMID:16894197</ref> NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication.<ref>PMID:16894197</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 22:
	[[Category: Hepatitis c virus]]		[[Category: Hepatitis c virus]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Deng, L.]]	+	[[Category: Deng, L]]
-	[[Category: Zhang, P.]]	+	[[Category: Zhang, P]]
	[[Category: Anti-hcv e2]]		[[Category: Anti-hcv e2]]
	[[Category: Antibody]]		[[Category: Antibody]]
	[[Category: Hcv e2]]		[[Category: Hcv e2]]
	[[Category: Immune system-viral protein complex]]		[[Category: Immune system-viral protein complex]]

OCA at 06:46, 23 July 2014

2014-07-23T06:46:53Z

←Older revision		Revision as of 06:46, 23 July 2014
Line 6:		Line 6:
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [http://www.ebi.ac.uk/pdbsum/4q0x PDBsum]</span></td></tr>		<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [http://www.ebi.ac.uk/pdbsum/4q0x PDBsum]</span></td></tr>
	<table>		<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The X-ray crystal structure of epitope II on the E2 protein of hepatitis C virus, in complex with nonneutralizing antibody mAb#12, has been solved at 2.90-A resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal alpha-helix and the N-terminal loop) was found to deviate significantly from that observed in those corresponding complexes with neutralizing antibodies. The distinct conformations are mediated largely by the flexibility of a highly conserved glycine residue that connects these components. Thus, it is the particular tertiary structure of epitope II, which is presented in a spatial and temporal manner, that determines the specificity of antibody recognition and, consequently, the outcome of neutralization or nonneutralization.
		+
		+	Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization.,Deng L, Ma L, Virata-Theimer ML, Zhong L, Yan H, Zhao Z, Struble E, Feinstone S, Alter H, Zhang P Proc Natl Acad Sci U S A. 2014 Jul 7. pii: 201411317. PMID:25002515<ref>PMID:25002515</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:33, 9 July 2014

2014-07-09T07:33:52Z

←Older revision		Revision as of 07:33, 9 July 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2==
-		+	<StructureSection load='4q0x' size='340' side='right' caption='[[4q0x]], [[Resolution\|resolution]] 2.90Å' scene=''>
-	~~The entry~~ 4q0x is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4q0x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0X FirstGlance]. <br>
-	~~Authors~~: Deng, L., Zhang, P.	+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hzl\|4hzl]]</td></tr>
-		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [http://www.ebi.ac.uk/pdbsum/4q0x PDBsum]</span></td></tr>
-	~~Description~~: ~~Crystal structure of non~~-~~neutralizing antibody in~~ complex ~~with Epitope II of HCV E2~~	+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Hepatitis c virus]]
		+	[[Category: Mus musculus]]
		+	[[Category: Deng, L.]]
		+	[[Category: Zhang, P.]]
		+	[[Category: Anti-hcv e2]]
		+	[[Category: Antibody]]
		+	[[Category: Hcv e2]]
		+	[[Category: Immune system-viral protein complex]]

OCA at 09:09, 16 April 2014

2014-04-16T09:09:38Z

←Older revision		Revision as of 09:09, 16 April 2014
Line 3:		Line 3:
	The entry 4q0x is ON HOLD		The entry 4q0x is ON HOLD

-	Authors: Deng, L., Zhang, P	+	Authors: Deng, L., Zhang, P.

	Description: Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2		Description: Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2

OCA: Protected "4q0x" [edit=sysop:move=sysop]

2014-04-09T06:00:41Z

Protected "4q0x" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:00, 9 April 2014

OCA: New page: '''Unreleased structure''' The entry 4q0x is ON HOLD Authors: Deng, L., Zhang, P Description: Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2

2014-04-09T06:00:40Z

New page: '''Unreleased structure''' The entry 4q0x is ON HOLD Authors: Deng, L., Zhang, P Description: Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2

New page

'''Unreleased structure'''

The entry 4q0x is ON HOLD

Authors: Deng, L., Zhang, P

Description: Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2