View source for 1bvp


==THE CRYSTAL STRUCTURE OF BLUETONGUE VIRUS VP7==
<StructureSection load='1bvp' size='340' side='right'caption='[[1bvp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bvp]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BVP 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=1bvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvp OCA], [http://pdbe.org/1bvp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bvp RCSB], [http://www.ebi.ac.uk/pdbsum/1bvp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bvp ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/VP7_BTV10 VP7_BTV10]] The VP7 protein is one of the five proteins (with VP1, VP3, VP4, and VP6) which form the inner capsid of the virus. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/1bvp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bvp ConSurf].
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== Publication Abstract from PubMed ==
Bluetongue virus (BTV), a representative of the orbivirus genus of the Reoviridae, is considerably larger (at 80 nm across), and structurally more complex, than any virus for which we have comprehensive structural information. Orbiviruses infect mammalian hosts through insect vectors and cause economically important diseases of domesticated animals. They possess a segmented double-stranded RNA genome within a capsid composed of four major types of polypeptide chains. An outer layer of VP2 and VP5 is removed as the virus enters the target cell, to leave an intact core within the cell. This core is 70 nm across and composed of 780 copies of VP7 (M(r) 38K) that, as trimers, form 260 'bristly' capsomeres clothing an inner scaffold constructed from VP3 (M(r) 103K). We report here the crystal structure of VP7 from BTV serotype 10, which reveals a molecular architecture not seen previously in viral structural proteins. Each subunit consists of two domains, one a beta-sandwich, the other a bundle of alpha-helices, and a short carboxy-terminal arm which might tie trimers together during capsid formation. A concentration of methionine residues at the core of the molecule could provide plasticity, relieving structural mismatches during assembly.

The crystal structure of bluetongue virus VP7.,Grimes J, Basak AK, Roy P, Stuart D Nature. 1995 Jan 12;373(6510):167-70. PMID:7816101<ref>PMID:7816101</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Virus coat protein|Virus coat protein]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Grimes, J]]
[[Category: Stuart, D]]
[[Category: Trimer]]
[[Category: Viral protein]]
[[Category: Virus]]
[[Category: Vp7]]