4bbl: Difference between revisions
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==Cryo-electron microscopy reconstruction of the helical part of influenza A virus ribonucleoprotein isolated from virions.== | |||
<StructureSection load='4bbl' size='340' side='right' caption='[[4bbl]], [[Resolution|resolution]] 18.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bbl]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BBL FirstGlance]. <br> | |||
</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=4bbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bbl RCSB], [http://www.ebi.ac.uk/pdbsum/4bbl PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The influenza viruses cause annual epidemics of respiratory disease and occasional pandemics, which constitute a major public-health issue. The segmented negative-stranded RNAs are associated with the polymerase complex and nucleoprotein (NP), forming ribonucleoproteins (RNPs), which are responsible for virus transcription and replication. We describe the structure of native RNPs derived from virions. They show a double-helical conformation in which two NP strands of opposite polarity are associated with each other along the helix. Both strands are connected by a short loop at one end of the particle and interact with the polymerase complex at the other end. This structure will be relevant for unraveling the mechanisms of nuclear import of parental virus RNPs, their transcription and replication, and the encapsidation of progeny RNPs into virions. | |||
The structure of native influenza virion ribonucleoproteins.,Arranz R, Coloma R, Chichon FJ, Conesa JJ, Carrascosa JL, Valpuesta JM, Ortin J, Martin-Benito J Science. 2012 Dec 21;338(6114):1634-7. doi: 10.1126/science.1228172. Epub 2012, Nov 22. PMID:23180776<ref>PMID:23180776</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Nucleoprotein|Nucleoprotein]] | *[[Nucleoprotein|Nucleoprotein]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Influenza a virus]] | [[Category: Influenza a virus]] | ||
[[Category: Arranz, R | [[Category: Arranz, R]] | ||
[[Category: Carrascosa, J L | [[Category: Carrascosa, J L]] | ||
[[Category: Chichon, F J | [[Category: Chichon, F J]] | ||
[[Category: Coloma, R | [[Category: Coloma, R]] | ||
[[Category: Conesa, J J | [[Category: Conesa, J J]] | ||
[[Category: Martin-Benito, J | [[Category: Martin-Benito, J]] | ||
[[Category: Ortin, J | [[Category: Ortin, J]] | ||
[[Category: Valpuesta, J M | [[Category: Valpuesta, J M]] | ||
[[Category: Nuclear protein]] | [[Category: Nuclear protein]] | ||
[[Category: Nucleocapsid]] | [[Category: Nucleocapsid]] | ||
Revision as of 11:37, 18 December 2014
Cryo-electron microscopy reconstruction of the helical part of influenza A virus ribonucleoprotein isolated from virions.Cryo-electron microscopy reconstruction of the helical part of influenza A virus ribonucleoprotein isolated from virions.
Structural highlights
Publication Abstract from PubMedThe influenza viruses cause annual epidemics of respiratory disease and occasional pandemics, which constitute a major public-health issue. The segmented negative-stranded RNAs are associated with the polymerase complex and nucleoprotein (NP), forming ribonucleoproteins (RNPs), which are responsible for virus transcription and replication. We describe the structure of native RNPs derived from virions. They show a double-helical conformation in which two NP strands of opposite polarity are associated with each other along the helix. Both strands are connected by a short loop at one end of the particle and interact with the polymerase complex at the other end. This structure will be relevant for unraveling the mechanisms of nuclear import of parental virus RNPs, their transcription and replication, and the encapsidation of progeny RNPs into virions. The structure of native influenza virion ribonucleoproteins.,Arranz R, Coloma R, Chichon FJ, Conesa JJ, Carrascosa JL, Valpuesta JM, Ortin J, Martin-Benito J Science. 2012 Dec 21;338(6114):1634-7. doi: 10.1126/science.1228172. Epub 2012, Nov 22. PMID:23180776[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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