1i9w

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(New page: 200px<br /><applet load="1i9w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i9w, resolution 3.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1i9w.gif|left|200px]]<br /><applet load="1i9w" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1i9w, resolution 3.0&Aring;" />
caption="1i9w, resolution 3.0&Aring;" />
'''CRYSTAL STRUCTURE OF THE FUSION GLYCOPROTEIN E1 FROM SEMLIKI FOREST VIRUS'''<br />
'''CRYSTAL STRUCTURE OF THE FUSION GLYCOPROTEIN E1 FROM SEMLIKI FOREST VIRUS'''<br />
==Overview==
==Overview==
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Semliki Forest virus (SFV) has been extensively studied as a model for, analyzing entry of enveloped viruses into target cells. Here we describe, the trace of the polypeptide chain of the SFV fusion glycoprotein, E1, derived from an electron density map at 3.5 A resolution and describe its, interactions at the surface of the virus. E1 is unexpectedly similar to, the flavivirus envelope protein, with three structural domains disposed in, the same primary sequence arrangement. These results introduce a new class, of membrane fusion proteins which display lateral interactions to induce, the necessary curvature and direct budding of closed particles. The, resulting surface protein lattice is primed to cause membrane fusion when, exposed to the acidic environment of the endosome.
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Semliki Forest virus (SFV) has been extensively studied as a model for analyzing entry of enveloped viruses into target cells. Here we describe the trace of the polypeptide chain of the SFV fusion glycoprotein, E1, derived from an electron density map at 3.5 A resolution and describe its interactions at the surface of the virus. E1 is unexpectedly similar to the flavivirus envelope protein, with three structural domains disposed in the same primary sequence arrangement. These results introduce a new class of membrane fusion proteins which display lateral interactions to induce the necessary curvature and direct budding of closed particles. The resulting surface protein lattice is primed to cause membrane fusion when exposed to the acidic environment of the endosome.
==About this Structure==
==About this Structure==
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1I9W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Semliki_forest_virus Semliki forest virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I9W OCA].
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1I9W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Semliki_forest_virus Semliki forest virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9W OCA].
==Reference==
==Reference==
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[[Category: Semliki forest virus]]
[[Category: Semliki forest virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Fuller, S.D.]]
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[[Category: Fuller, S D.]]
[[Category: Lescar, J.]]
[[Category: Lescar, J.]]
[[Category: Navaza, J.]]
[[Category: Navaza, J.]]
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[[Category: Rey, F.A.]]
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[[Category: Rey, F A.]]
[[Category: Roussel, A.]]
[[Category: Roussel, A.]]
[[Category: Wengler, G.]]
[[Category: Wengler, G.]]
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[[Category: Wien, M.W.]]
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[[Category: Wien, M W.]]
[[Category: envelope glycoprotein]]
[[Category: envelope glycoprotein]]
[[Category: membrane fusion]]
[[Category: membrane fusion]]
[[Category: virus]]
[[Category: virus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:12:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:32 2008''

Revision as of 11:09, 21 February 2008


1i9w, resolution 3.0Å

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CRYSTAL STRUCTURE OF THE FUSION GLYCOPROTEIN E1 FROM SEMLIKI FOREST VIRUS

Overview

Semliki Forest virus (SFV) has been extensively studied as a model for analyzing entry of enveloped viruses into target cells. Here we describe the trace of the polypeptide chain of the SFV fusion glycoprotein, E1, derived from an electron density map at 3.5 A resolution and describe its interactions at the surface of the virus. E1 is unexpectedly similar to the flavivirus envelope protein, with three structural domains disposed in the same primary sequence arrangement. These results introduce a new class of membrane fusion proteins which display lateral interactions to induce the necessary curvature and direct budding of closed particles. The resulting surface protein lattice is primed to cause membrane fusion when exposed to the acidic environment of the endosome.

About this Structure

1I9W is a Single protein structure of sequence from Semliki forest virus. Full crystallographic information is available from OCA.

Reference

The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH., Lescar J, Roussel A, Wien MW, Navaza J, Fuller SD, Wengler G, Wengler G, Rey FA, Cell. 2001 Apr 6;105(1):137-48. PMID:11301009

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