1urz

From Proteopedia

Revision as of 02:13, 25 November 2007

LOW PH INDUCED, MEMBRANE FUSION CONFORMATION OF THE ENVELOPE PROTEIN OF TICK-BORNE ENCEPHALITIS VIRUS

Overview

Enveloped viruses enter cells via a membrane fusion reaction driven by, conformational changes of specific viral envelope proteins. We report here, the structure of the ectodomain of the tick-borne encephalitis virus, envelope glycoprotein, E, a prototypical class II fusion protein, in its, trimeric low-pH-induced conformation. We show that, in the conformational, transition, the three domains of the neutral-pH form are maintained but, their relative orientation is altered. Similar to the postfusion class I, proteins, the subunits rearrange such that the fusion peptide loops, cluster at one end of an elongated molecule and the C-terminal segments, connecting to the viral transmembrane region, run along the sides of the, trimer pointing toward the fusion peptide loops. Comparison with the, low-pH-induced form of the alphavirus class II fusion protein reveals, striking differences at the end of the molecule bearing the fusion, peptides, suggesting an important conformational effect of the missing, membrane connecting segment.

About this Structure

1URZ is a Single protein structure of sequence from Tick-borne encephalitis virus. Full crystallographic information is available from OCA.

Reference

Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation., Bressanelli S, Stiasny K, Allison SL, Stura EA, Duquerroy S, Lescar J, Heinz FX, Rey FA, EMBO J. 2004 Feb 25;23(4):728-38. Epub 2004 Feb 12. PMID:14963486

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