1urz
From Proteopedia
(New page: 200px<br /><applet load="1urz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1urz, resolution 2.7Å" /> '''LOW PH INDUCED, MEMBR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1urz.gif|left|200px]]<br /><applet load="1urz" size=" | + | [[Image:1urz.gif|left|200px]]<br /><applet load="1urz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1urz, resolution 2.7Å" /> | caption="1urz, resolution 2.7Å" /> | ||
'''LOW PH INDUCED, MEMBRANE FUSION CONFORMATION OF THE ENVELOPE PROTEIN OF TICK-BORNE ENCEPHALITIS VIRUS'''<br /> | '''LOW PH INDUCED, MEMBRANE FUSION CONFORMATION OF THE ENVELOPE PROTEIN OF TICK-BORNE ENCEPHALITIS VIRUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Enveloped viruses enter cells via a membrane fusion reaction driven by | + | 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== | ==About this Structure== | ||
| - | 1URZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tick-borne_encephalitis_virus Tick-borne encephalitis virus]. Full crystallographic information is available from [http:// | + | 1URZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tick-borne_encephalitis_virus Tick-borne encephalitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URZ OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Tick-borne encephalitis virus]] | [[Category: Tick-borne encephalitis virus]] | ||
[[Category: Bressanelli, S.]] | [[Category: Bressanelli, S.]] | ||
| - | [[Category: Rey, F | + | [[Category: Rey, F A.]] |
[[Category: envelope protein]] | [[Category: envelope protein]] | ||
[[Category: membrane fusion]] | [[Category: membrane fusion]] | ||
[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:38 2008'' |
Revision as of 13:27, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 15:27:38 2008
