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1thd
From Proteopedia
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| - | [[ | + | ==COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION== |
| + | <StructureSection load='1thd' size='340' side='right' caption='[[1thd]], [[Resolution|resolution]] 9.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1thd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2_puerto_rico/pr159-s1/1969 Dengue virus 2 puerto rico/pr159-s1/1969]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1THD FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tg8|1tg8]], [[1p58|1p58]]</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=1thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1thd RCSB], [http://www.ebi.ac.uk/pdbsum/1thd PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dengue virus, a member of the Flaviviridae family, has a surface composed of 180 copies each of the envelope (E) glycoprotein and the membrane (M) protein. The crystal structure of an N-terminal fragment of E has been determined and compared with a previously described structure. The primary difference between these structures is a 10 degrees rotation about a hinge relating the fusion domain DII to domains DI and DIII. These two rigid body components were used for independent fitting of E into the cryo-electron microscopy maps of both immature and mature dengue viruses. The fitted E structures in these two particles showed a difference of 27 degrees between the two components. Comparison of the E structure in its postfusion state with that in the immature and mature virions shows a rotation approximately around the same hinge. Flexibility of E is apparently a functional requirement for assembly and infection of flaviviruses. | ||
| - | + | Conformational changes of the flavivirus E glycoprotein.,Zhang Y, Zhang W, Ogata S, Clements D, Strauss JH, Baker TS, Kuhn RJ, Rossmann MG Structure. 2004 Sep;12(9):1607-18. PMID:15341726<ref>PMID:15341726</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Dengue virus 2 puerto rico/pr159-s1/1969]] | |
| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Baker, T S.]] | [[Category: Baker, T S.]] | ||
[[Category: Clements, D.]] | [[Category: Clements, D.]] | ||
Revision as of 11:23, 20 October 2014
COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION
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