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3vbf

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Revision as of 22:46, 5 August 2016

Crystal structure of formaldehyde treated human Enterovirus 71 (space group I23)

Structural highlights

3vbf is a 4 chain structure with sequence from Ev-71. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	3vbh, 3vbo, 3vbr, 3vbs, 3vbu
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71. Nat Struct Mol Biol. 2012 Mar 4. doi: 10.1038/nsmb.2255. PMID:22388738 doi:10.1038/nsmb.2255

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vbf"

@@ Line 1: / Line 1: @@
 ==Crystal structure of formaldehyde treated human Enterovirus 71 (space group I23)==
 <StructureSection load='3vbf' size='340' side='right' caption='[[3vbf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3vbf]] is a 4 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=3VBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VBF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3vbf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ev-71 Ev-71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VBF FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SPH:SPHINGOSINE'>SPH</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vbh|3vbh]], [[3vbo|3vbo]], [[3vbr|3vbr]], [[3vbs|3vbs]], [[3vbu|3vbu]]</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=3vbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vbf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vbf RCSB], [http://www.ebi.ac.uk/pdbsum/3vbf 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=3vbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vbf OCA], [http://pdbe.org/3vbf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vbf RCSB], [http://www.ebi.ac.uk/pdbsum/3vbf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vbf ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3vbf" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 24: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Human enterovirus 71]]
+[[Category: Ev-71]]
 [[Category: Axford, D]]
 [[Category: Evans, G]]

3vbf

From Proteopedia

Revision as of 22:46, 5 August 2016

Crystal structure of formaldehyde treated human Enterovirus 71 (space group I23)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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