3vbu: Difference between revisions
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[[ | ==Crystal structure of empty human Enterovirus 71 particle== | ||
<StructureSection load='3vbu' size='340' side='right' caption='[[3vbu]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vbu]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VBU FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vbf|3vbf]], [[3vbh|3vbh]], [[3vbo|3vbo]], [[3vbr|3vbr]], [[3vbs|3vbs]]</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=3vbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vbu RCSB], [http://www.ebi.ac.uk/pdbsum/3vbu PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/B2ZUN0_9ENTO B2ZUN0_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 == | |||
Enterovirus 71 (EV71) is a major agent of hand, foot and mouth disease in children that can cause severe central nervous system disease and death. No vaccine or antiviral therapy is available. High-resolution structural analysis of the mature virus and natural empty particles shows that the mature virus is structurally similar to other enteroviruses. In contrast, the empty particles are markedly expanded and resemble elusive enterovirus-uncoating intermediates not previously characterized in atomic detail. Hydrophobic pockets in the EV71 capsid are collapsed in this expanded particle, providing a detailed explanation of the mechanism for receptor-binding triggered virus uncoating. These structures provide a model for enterovirus uncoating in which the VP1 GH loop acts as an adaptor-sensor for cellular receptor attachment, converting heterologous inputs to a generic uncoating mechanism, highlighting new opportunities for therapeutic intervention. | |||
A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71.,Wang X, Peng W, Ren J, Hu Z, Xu J, Lou Z, Li X, Yin W, Shen X, Porta C, Walter TS, Evans G, Axford D, Owen R, Rowlands DJ, Wang J, Stuart DI, Fry EE, Rao Z Nat Struct Mol Biol. 2012 Mar 4. doi: 10.1038/nsmb.2255. PMID:22388738<ref>PMID:22388738</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Virus coat protein|Virus coat protein]] | *[[Virus coat protein|Virus coat protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Human enterovirus 71]] | [[Category: Human enterovirus 71]] | ||
[[Category: Axford, D | [[Category: Axford, D]] | ||
[[Category: Evans, G | [[Category: Evans, G]] | ||
[[Category: Fry, E E | [[Category: Fry, E E]] | ||
[[Category: Hu, Z | [[Category: Hu, Z]] | ||
[[Category: Li, X | [[Category: Li, X]] | ||
[[Category: Lou, Z | [[Category: Lou, Z]] | ||
[[Category: Owen, R | [[Category: Owen, R]] | ||
[[Category: Peng, W | [[Category: Peng, W]] | ||
[[Category: Porta, C | [[Category: Porta, C]] | ||
[[Category: Rao, Z | [[Category: Rao, Z]] | ||
[[Category: Ren, J | [[Category: Ren, J]] | ||
[[Category: Rowlands, D J | [[Category: Rowlands, D J]] | ||
[[Category: Shen, X | [[Category: Shen, X]] | ||
[[Category: Stuart, D I | [[Category: Stuart, D I]] | ||
[[Category: Walter, T S | [[Category: Walter, T S]] | ||
[[Category: Wang, J | [[Category: Wang, J]] | ||
[[Category: Wang, X | [[Category: Wang, X]] | ||
[[Category: Xu, J | [[Category: Xu, J]] | ||
[[Category: Yin, W | [[Category: Yin, W]] | ||
[[Category: Adaptor-sensor]] | [[Category: Adaptor-sensor]] | ||
[[Category: Enterovirus uncoating]] | [[Category: Enterovirus uncoating]] | ||
Revision as of 15:18, 25 December 2014
Crystal structure of empty human Enterovirus 71 particleCrystal structure of empty human Enterovirus 71 particle
Structural highlights
Function[B2ZUN0_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] Publication Abstract from PubMedEnterovirus 71 (EV71) is a major agent of hand, foot and mouth disease in children that can cause severe central nervous system disease and death. No vaccine or antiviral therapy is available. High-resolution structural analysis of the mature virus and natural empty particles shows that the mature virus is structurally similar to other enteroviruses. In contrast, the empty particles are markedly expanded and resemble elusive enterovirus-uncoating intermediates not previously characterized in atomic detail. Hydrophobic pockets in the EV71 capsid are collapsed in this expanded particle, providing a detailed explanation of the mechanism for receptor-binding triggered virus uncoating. These structures provide a model for enterovirus uncoating in which the VP1 GH loop acts as an adaptor-sensor for cellular receptor attachment, converting heterologous inputs to a generic uncoating mechanism, highlighting new opportunities for therapeutic intervention. A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71.,Wang X, Peng W, Ren J, Hu Z, Xu J, Lou Z, Li X, Yin W, Shen X, Porta C, Walter TS, Evans G, Axford D, Owen R, Rowlands DJ, Wang J, Stuart DI, Fry EE, Rao Z Nat Struct Mol Biol. 2012 Mar 4. doi: 10.1038/nsmb.2255. PMID:22388738[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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