1thd
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(New page: 200px<br /><applet load="1thd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1thd" /> '''COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTE...)
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Revision as of 01:08, 21 November 2007
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COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION
Overview
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.
About this Structure
1THD is a Single protein structure of sequence from Dengue virus type 3. Full crystallographic information is available from OCA.
Reference
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
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