1es6
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(New page: 200px<br /><applet load="1es6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1es6, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 12:08, 20 November 2007
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CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS
Overview
Ebola virus maturation occurs at the plasma membrane of infected cells and, involves the clustering of the viral matrix protein VP40 at the assembly, site as well as its interaction with the lipid bilayer. Here we report the, X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The, crystal structure reveals that Ebola virus VP40 is topologically distinct, from all other known viral matrix proteins, consisting of two domains with, unique folds, connected by a flexible linker. The C-terminal domain, which, is absolutely required for membrane binding, contains large hydrophobic, patches that may be involved in the interaction with lipid bilayers., Likewise, a highly basic region is shared between the two domains. The, crystal structure reveals how the molecule may be able to switch from a, monomeric conformation to a hexameric form, as observed in vitro. Its, implications for the assembly process are discussed.
About this Structure
1ES6 is a Single protein structure of sequence from Ebola virus sp.. Full crystallographic information is available from OCA.
Reference
Crystal structure of the matrix protein VP40 from Ebola virus., Dessen A, Volchkov V, Dolnik O, Klenk HD, Weissenhorn W, EMBO J. 2000 Aug 15;19(16):4228-36. PMID:10944105
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