4c0u - Revision history

OCA at 11:07, 9 May 2024

OCA — Thu, 09 May 2024 11:07:24 GMT

←Older revision		Revision as of 11:07, 9 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterovirus_A71 Enterovirus A71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0U FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterovirus_A71 Enterovirus A71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0U 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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [https://pdbe.org/4c0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [https://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 10Å</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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [https://pdbe.org/4c0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [https://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/A9X4C2_HE71 A9X4C2_HE71]] Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions.[ARBA:ARBA00024846] Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step.[RuleBase:RU364118] Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks.[RuleBase:RU364118] Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[RuleBase:RU364118] Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[RuleBase:RU364118] Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm.[RuleBase:RU364118] Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step.[ARBA:ARBA00025202] Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[ARBA:ARBA00025306] Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm.[ARBA:ARBA00024643] Protease 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins.[RuleBase:RU364118] Protease 3C: Major viral protease that mediates proteolytic processing of the polyprotein. Cleaves host EIF5B, contributing to host translation shutoff. Cleaves also host PABPC1, contributing to host translation shutoff.[RuleBase:RU364118] Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.[RuleBase:RU364118] Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.[RuleBase:RU364118] Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface.[RuleBase:RU364118] Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.[RuleBase:RU364118] Protein 3CD: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome.[RuleBase:RU364118] RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.[RuleBase:RU364118] Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.[RuleBase:RU364118]	+	[https://www.uniprot.org/uniprot/A9X4C2_HE71 A9X4C2_HE71] Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions.[ARBA:ARBA00024846] Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step.[RuleBase:RU364118] Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks.[RuleBase:RU364118] Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[RuleBase:RU364118] Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[RuleBase:RU364118] Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm.[RuleBase:RU364118] Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step.[ARBA:ARBA00025202] Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[ARBA:ARBA00025306] Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm.[ARBA:ARBA00024643] Protease 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins.[RuleBase:RU364118] Protease 3C: Major viral protease that mediates proteolytic processing of the polyprotein. Cleaves host EIF5B, contributing to host translation shutoff. Cleaves also host PABPC1, contributing to host translation shutoff.[RuleBase:RU364118] Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.[RuleBase:RU364118] Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.[RuleBase:RU364118] Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface.[RuleBase:RU364118] Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.[RuleBase:RU364118] Protein 3CD: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome.[RuleBase:RU364118] RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.[RuleBase:RU364118] Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.[RuleBase:RU364118]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Antibodies were prepared by immunizing mice with empty, immature particles of human enterovirus 71 (EV71), a picornavirus that causes severe neurological disease in young children. The capsid structure of these empty particles is different from that of the mature virus and is similar to "A" particles encountered when picornaviruses recognize a potential host cell before genome release. The monoclonal antibody E18, generated by this immunization, induced a conformational change when incubated at temperatures between 4 degrees C and 37 degrees C with mature virus, transforming infectious virions into A particles. The resultant loss of genome that was observed by cryo-EM and a fluorescent SYBR Green dye assay inactivated the virus, establishing the mechanism by which the virus is inactivated and demonstrating that the E18 antibody has potential as an anti-EV71 therapy. The antibody-mediated virus neutralization by the induction of genome release has not been previously demonstrated. Furthermore, the present results indicate that antibodies with genome-release activity could also be produced for other picornaviruses by immunization with immature particles.
		+
		+	Neutralizing antibodies can initiate genome release from human enterovirus 71.,Plevka P, Lim PY, Perera R, Cardosa J, Suksatu A, Kuhn RJ, Rossmann MG Proc Natl Acad Sci U S A. 2014 Jan 27. PMID:24469789<ref>PMID:24469789</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c0u" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Virus coat proteins 3D structures\|Virus coat proteins 3D structures]]		*[[Virus coat proteins 3D structures\|Virus coat proteins 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</SX>		</SX>

OCA at 17:19, 7 September 2022

OCA — Wed, 07 Sep 2022 17:19:45 GMT

←Older revision		Revision as of 17:19, 7 September 2022
Line 3:		Line 3:
	<SX load='4c0u' size='340' side='right' viewer='molstar' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>		<SX load='4c0u' size='340' side='right' viewer='molstar' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human_enterovirus_71 Human enterovirus 71~~] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=4C0U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterovirus_A71 Enterovirus A71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0U FirstGlance]. <br>
-	</td></tr>~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [https://pdbe.org/4c0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [https://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u ProSAT]</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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [~~http~~://pdbe.org/4c0u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/~~A9X4C2_9ENTO A9X4C2_9ENTO~~]] ~~Protein 2C associates with~~ and ~~induces structural rearrangements of intracellular membranes~~. ~~It displays~~ RNA-~~binding~~, ~~nucleotide binding and NTPase activities~~ (By similarity).[~~SAAS~~:~~SAAS000199_004_016611~~] ~~Protein 3C~~ is ~~a cysteine protease that generates mature viral~~ proteins ~~from~~ the ~~precursor polyprotein~~. ~~In addition~~ to its ~~proteolytic activity~~, ~~it binds~~ to viral RNA, and ~~thus influences~~ viral genome ~~replication~~. ~~RNA and substrate bind co-operatively~~ to the ~~protease~~ (By similarity).[~~SAAS~~:~~SAAS000199_004_042266~~] ~~RNA-directed RNA polymerase 3D-POL replicates genomic~~ and ~~antigenomic RNA by recognizing replications specific signals~~ (By similarity).[~~SAAS~~:~~SAAS000199_004_010047~~]	+	[[https://www.uniprot.org/uniprot/A9X4C2_HE71 A9X4C2_HE71]] Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions.[ARBA:ARBA00024846] Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step.[RuleBase:RU364118] Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks.[RuleBase:RU364118] Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[RuleBase:RU364118] Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[RuleBase:RU364118] Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm.[RuleBase:RU364118] Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step.[ARBA:ARBA00025202] Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[ARBA:ARBA00025306] Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm.[ARBA:ARBA00024643] Protease 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins.[RuleBase:RU364118] Protease 3C: Major viral protease that mediates proteolytic processing of the polyprotein. Cleaves host EIF5B, contributing to host translation shutoff. Cleaves also host PABPC1, contributing to host translation shutoff.[RuleBase:RU364118] Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.[RuleBase:RU364118] Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.[RuleBase:RU364118] Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface.[RuleBase:RU364118] Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.[RuleBase:RU364118] Protein 3CD: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome.[RuleBase:RU364118] RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.[RuleBase:RU364118] Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.[RuleBase:RU364118]
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	~~Antibodies were prepared by immunizing mice with empty, immature particles~~ of ~~human enterovirus 71~~ (~~EV71~~), a ~~picornavirus that causes severe neurological disease~~ in ~~young children. The capsid structure of these empty particles~~ is ~~different from~~ that of the ~~mature virus and is similar~~ to ~~"A" particles encountered when picornaviruses recognize~~ a ~~potential~~ host cell ~~before genome release~~. ~~The monoclonal antibody E18~~, ~~generated by this immunization~~, ~~induced a conformational change when incubated at temperatures between 4 degrees C~~ and ~~37 degrees C~~ with ~~mature virus~~, ~~transforming infectious virions into A particles~~. ~~The resultant loss of genome that was observed~~ by ~~cryo~~-EM and ~~a fluorescent SYBR Green dye assay inactivated~~ the ~~virus~~, ~~establishing~~ the ~~mechanism by which~~ the ~~virus~~ is ~~inactivated~~ and ~~demonstrating~~ that the ~~E18 antibody has potential as an anti-EV71 therapy~~. ~~The antibody~~-~~mediated virus neutralization by~~ the ~~induction~~ of genome ~~release has not been previously demonstrated~~. ~~Furthermore~~, ~~the present results indicate that antibodies with~~ genome-~~release activity could also be produced~~ for ~~other picornaviruses~~ by ~~immunization with immature particles~~.	+

-	Neutralizing antibodies can initiate genome release from human enterovirus 71.,Plevka P, Lim PY, Perera R, Cardosa J, Suksatu A, Kuhn RJ, Rossmann MG Proc Natl Acad Sci U S A. 2014 Jan 27. PMID:24469789<ref>PMID:24469789</ref>	+	==See Also==
-		+	*[[Virus coat proteins 3D structures\|Virus coat proteins 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4c0u" style="background-color:#fffaf0;"></div>~~	+
-	== ~~References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: ~~Human enterovirus 71~~]]	+	[[Category: Enterovirus A71]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Cardosa, J]]	+	[[Category: Cardosa J]]
-	[[Category: Kuhn~~, R J~~]]	+	[[Category: Kuhn RJ]]
-	[[Category: Perera, R]]	+	[[Category: Perera R]]
-	[[Category: Plevka, P]]	+	[[Category: Plevka P]]
-	[[Category: Rossmann~~, M G~~]]	+	[[Category: Rossmann MG]]
-	[[Category: Suksatu, A]]	+	[[Category: Suksatu A]]
-	~~[[Category: Ev71]]~~	+
-	~~[[Category: Pathogen]]~~	+
-	~~[[Category: Virus]]~~	+
-	~~[[Category: Virus-immune system complex~~]]	+

OCA at 18:58, 10 April 2020

OCA — Fri, 10 Apr 2020 18:58:46 GMT

←Older revision		Revision as of 18:58, 10 April 2020
Line 3:		Line 3:
	<SX load='4c0u' size='340' side='right' viewer='molstar' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>		<SX load='4c0u' size='340' side='right' viewer='molstar' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C0U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4C0U FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [http://pdbe.org/4c0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [http://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u ProSAT]</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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [http://pdbe.org/4c0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [http://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:52, 6 March 2020

OCA — Fri, 06 Mar 2020 17:52:18 GMT

←Older revision		Revision as of 17:52, 6 March 2020
Line 1:		Line 1:

	==Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18==		==Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18==
-	<~~StructureSection~~ load='4c0u' size='340' side='right'caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>	+	<SX load='4c0u' size='340' side='right' viewer='molstar' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>
Line 21:		Line 21:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Human enterovirus 71]]		[[Category: Human enterovirus 71]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 06:18, 21 August 2019

OCA — Wed, 21 Aug 2019 06:18:12 GMT

←Older revision		Revision as of 06:18, 21 August 2019
Line 1:		Line 1:

	==Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18==		==Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18==
-	<StructureSection load='4c0u' size='340' side='right' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>	+	<StructureSection load='4c0u' size='340' side='right'caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Human enterovirus 71]]		[[Category: Human enterovirus 71]]
		+	[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Cardosa, J]]		[[Category: Cardosa, J]]

OCA at 22:18, 15 November 2017

OCA — Wed, 15 Nov 2017 22:18:43 GMT

←Older revision		Revision as of 22:18, 15 November 2017
Line 3:		Line 3:
	<StructureSection load='4c0u' size='340' side='right' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>		<StructureSection load='4c0u' size='340' side='right' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Ev-71 Ev-~~71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [http://pdbe.org/4c0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [http://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u 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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [http://pdbe.org/4c0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [http://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u ProSAT]</span></td></tr>
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ev-~~71]]	+	[[Category: Human enterovirus 71]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Cardosa, J]]		[[Category: Cardosa, J]]

OCA at 17:53, 4 August 2016

OCA — Thu, 04 Aug 2016 17:53:03 GMT

←Older revision		Revision as of 17:53, 4 August 2016
Line 1:		Line 1:
		+
	==Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18==		==Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18==
	<StructureSection load='4c0u' size='340' side='right' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>		<StructureSection load='4c0u' size='340' side='right' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Ev-71 Ev-71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Ev-71 Ev-71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [http://www.ebi.ac.uk/pdbsum/4c0u 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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [http://pdbe.org/4c0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [http://www.ebi.ac.uk/pdbsum/4c0u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0u 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 4c0u" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:37, 25 December 2014

OCA — Thu, 25 Dec 2014 11:37:34 GMT

←Older revision		Revision as of 11:37, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4c0u\| PDB=4c0u \| SCENE= }}~~	+	==Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18==
-	===Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18===	+	<StructureSection load='4c0u' size='340' side='right' caption='[[4c0u]], [[Resolution\|resolution]] 10.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24469789}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Ev-71 Ev-71] 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=4C0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0U FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=4c0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c0u RCSB], [http://www.ebi.ac.uk/pdbsum/4c0u PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/A9X4C2_9ENTO A9X4C2_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]		[[http://www.uniprot.org/uniprot/A9X4C2_9ENTO A9X4C2_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Antibodies were prepared by immunizing mice with empty, immature particles of human enterovirus 71 (EV71), a picornavirus that causes severe neurological disease in young children. The capsid structure of these empty particles is different from that of the mature virus and is similar to "A" particles encountered when picornaviruses recognize a potential host cell before genome release. The monoclonal antibody E18, generated by this immunization, induced a conformational change when incubated at temperatures between 4 degrees C and 37 degrees C with mature virus, transforming infectious virions into A particles. The resultant loss of genome that was observed by cryo-EM and a fluorescent SYBR Green dye assay inactivated the virus, establishing the mechanism by which the virus is inactivated and demonstrating that the E18 antibody has potential as an anti-EV71 therapy. The antibody-mediated virus neutralization by the induction of genome release has not been previously demonstrated. Furthermore, the present results indicate that antibodies with genome-release activity could also be produced for other picornaviruses by immunization with immature particles.

-	~~==About this Structure==~~	+	Neutralizing antibodies can initiate genome release from human enterovirus 71.,Plevka P, Lim PY, Perera R, Cardosa J, Suksatu A, Kuhn RJ, Rossmann MG Proc Natl Acad Sci U S A. 2014 Jan 27. PMID:24469789<ref>PMID:24469789</ref>
-	~~[[4c0u]] is a 5 chain structure with sequence~~ from ~~[http://en.wikipedia.org/wiki/Human_enterovirus_71 Human~~ enterovirus 71~~] 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=4C0U OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024469789</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: ~~Human enterovirus~~ 71]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ev-71]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Cardosa, J.]]	+	[[Category: Cardosa, J]]
-	[[Category: Kuhn, R J.]]	+	[[Category: Kuhn, R J]]
-	[[Category: Perera, R.]]	+	[[Category: Perera, R]]
-	[[Category: Plevka, P.]]	+	[[Category: Plevka, P]]
-	[[Category: Rossmann, M G.]]	+	[[Category: Rossmann, M G]]
-	[[Category: Suksatu, A.]]	+	[[Category: Suksatu, A]]
	[[Category: Ev71]]		[[Category: Ev71]]
	[[Category: Pathogen]]		[[Category: Pathogen]]
	[[Category: Virus]]		[[Category: Virus]]
	[[Category: Virus-immune system complex]]		[[Category: Virus-immune system complex]]

OCA at 11:24, 5 February 2014

OCA — Wed, 05 Feb 2014 11:24:27 GMT

←Older revision		Revision as of 11:24, 5 February 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4c0u\| PDB=4c0u \| SCENE= }}
		+	===Cryo-EM reconstruction of enterovirus 71 in complex with a neutralizing antibody E18===
		+	{{ABSTRACT_PUBMED_24469789}}

-	~~The entry 4c0u~~ is ~~ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/A9X4C2_9ENTO A9X4C2_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]

-	~~Authors~~: ~~Plevka, P~~.~~, Perera, R~~.~~, Cardosa, J~~.~~, Suksatu, A~~.~~, Kuhn, R~~.J.~~, Rossmann, M~~.G.	+	==About this Structure==
		+	[[4c0u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71] 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=4C0U OCA].

-	~~Description~~: ~~Cryo-EM reconstruction of~~ enterovirus 71 in complex ~~with a neutralizing antibody E18~~	+	==Reference==
		+	<ref group="xtra">PMID:024469789</ref><references group="xtra"/><references/>
		+	[[Category: Human enterovirus 71]]
		+	[[Category: Mus musculus]]
		+	[[Category: Cardosa, J.]]
		+	[[Category: Kuhn, R J.]]
		+	[[Category: Perera, R.]]
		+	[[Category: Plevka, P.]]
		+	[[Category: Rossmann, M G.]]
		+	[[Category: Suksatu, A.]]
		+	[[Category: Ev71]]
		+	[[Category: Pathogen]]
		+	[[Category: Virus]]
		+	[[Category: Virus-immune system complex]]

OCA: Protected "4c0u" [edit=sysop:move=sysop]

OCA — Wed, 14 Aug 2013 07:01:11 GMT

Protected "4c0u" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:01, 14 August 2013