2yew: Difference between revisions
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[[ | ==Modeling Barmah Forest virus structural proteins== | ||
<StructureSection load='2yew' size='340' side='right' caption='[[2yew]], [[Resolution|resolution]] 5.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2yew]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YEW FirstGlance]. <br> | |||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Togavirin Togavirin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.90 3.4.21.90] </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=2yew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yew OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yew RCSB], [http://www.ebi.ac.uk/pdbsum/2yew PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Barmah Forest virus (BFV) is a mosquito-borne alphavirus that infects humans. A 6-A-resolution cryo-electron microscopy three-dimensional structure of BFV exhibits a typical alphavirus organization, with RNA-containing nucleocapsid surrounded by a bilipid membrane anchored with the surface proteins E1 and E2. The map allows details of the transmembrane regions of E1 and E2 to be seen. The C-terminal end of the E2 transmembrane helix binds to the capsid protein. Following the E2 transmembrane helix, a short alpha-helical endodomain lies on the inner surface of the lipid envelope. The E2 endodomain interacts with E1 transmembrane helix from a neighboring E1-E2 trimeric spike, thereby acting as a spacer and a linker between spikes. In agreement with previous mutagenesis studies, the endodomain plays an important role in recruiting other E1-E2 spikes to the budding site during virus assembly. The E2 endodomain may thus serve as a target for antiviral drug design. | |||
The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions.,Kostyuchenko VA, Jakana J, Liu X, Haddow AD, Aung M, Weaver SC, Chiu W, Lok SM J Virol. 2011 Sep;85(18):9327-33. Epub 2011 Jul 13. PMID:21752915<ref>PMID:21752915</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Togavirin]] | [[Category: Togavirin]] | ||
[[Category: Aung, M.]] | [[Category: Aung, M.]] | ||
Revision as of 11:51, 29 October 2014
Modeling Barmah Forest virus structural proteins
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