1wyk

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(New page: 200px<br /><applet load="1wyk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wyk, resolution 2.0&Aring;" /> '''SINDBIS VIRUS CAPSID ...)
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[[Image:1wyk.jpg|left|200px]]<br /><applet load="1wyk" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1wyk.jpg|left|200px]]<br /><applet load="1wyk" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wyk, resolution 2.0&Aring;" />
caption="1wyk, resolution 2.0&Aring;" />
'''SINDBIS VIRUS CAPSID PROTEIN (114-264)'''<br />
'''SINDBIS VIRUS CAPSID PROTEIN (114-264)'''<br />
==Overview==
==Overview==
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Alphavirus budding from the plasma membrane is initiated by the specific, interaction of the nucleocapsid with the cytoplasmic domain of the, glycoprotein E2. It was proposed (Lee et al., Structure 4:531-541, 1996), that binding of the capsid protein residues 108 to 110 (the "N-terminal, arm" residues) to a hydrophobic pocket on the surface of the neighboring, capsid protein in the crystal structure mimics the binding of the E2, C-terminal residues into this pocket. In addition, structural comparisons, of wild-type and mutant Sindbis virus capsid protein (SCP) and Semliki, Forest virus capsid protein suggested that budding is associated with a, switch between two conformations of the hydrophobic pocket. To test the, proposed mechanism, SCP(114-264), which is missing the N-terminal arm, was, crystallized to examine the pocket conformation when the pocket is empty., However, the pocket was occupied by dioxane molecules from the, crystallization solution. The pocket conformation was the same as that, when it was occupied by the N-terminal arm, demonstrating that the pocket, favors binding ligands of appropriate size and shape.
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Alphavirus budding from the plasma membrane is initiated by the specific interaction of the nucleocapsid with the cytoplasmic domain of the glycoprotein E2. It was proposed (Lee et al., Structure 4:531-541, 1996) that binding of the capsid protein residues 108 to 110 (the "N-terminal arm" residues) to a hydrophobic pocket on the surface of the neighboring capsid protein in the crystal structure mimics the binding of the E2 C-terminal residues into this pocket. In addition, structural comparisons of wild-type and mutant Sindbis virus capsid protein (SCP) and Semliki Forest virus capsid protein suggested that budding is associated with a switch between two conformations of the hydrophobic pocket. To test the proposed mechanism, SCP(114-264), which is missing the N-terminal arm, was crystallized to examine the pocket conformation when the pocket is empty. However, the pocket was occupied by dioxane molecules from the crystallization solution. The pocket conformation was the same as that when it was occupied by the N-terminal arm, demonstrating that the pocket favors binding ligands of appropriate size and shape.
==About this Structure==
==About this Structure==
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1WYK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sindbis_virus Sindbis virus] with FOR and DIO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WYK OCA].
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1WYK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sindbis_virus Sindbis virus] with <scene name='pdbligand=FOR:'>FOR</scene> and <scene name='pdbligand=DIO:'>DIO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WYK OCA].
==Reference==
==Reference==
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[[Category: Sindbis virus]]
[[Category: Sindbis virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Kuhn, R.J.]]
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[[Category: Kuhn, R J.]]
[[Category: Lee, S.]]
[[Category: Lee, S.]]
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[[Category: Rossmann, M.G.]]
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[[Category: Rossmann, M G.]]
[[Category: DIO]]
[[Category: DIO]]
[[Category: FOR]]
[[Category: FOR]]
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[[Category: virus]]
[[Category: virus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:45:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:33 2008''

Revision as of 13:49, 21 February 2008

Image:1wyk.jpg

1wyk, resolution 2.0Å

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SINDBIS VIRUS CAPSID PROTEIN (114-264)

Overview

Alphavirus budding from the plasma membrane is initiated by the specific interaction of the nucleocapsid with the cytoplasmic domain of the glycoprotein E2. It was proposed (Lee et al., Structure 4:531-541, 1996) that binding of the capsid protein residues 108 to 110 (the "N-terminal arm" residues) to a hydrophobic pocket on the surface of the neighboring capsid protein in the crystal structure mimics the binding of the E2 C-terminal residues into this pocket. In addition, structural comparisons of wild-type and mutant Sindbis virus capsid protein (SCP) and Semliki Forest virus capsid protein suggested that budding is associated with a switch between two conformations of the hydrophobic pocket. To test the proposed mechanism, SCP(114-264), which is missing the N-terminal arm, was crystallized to examine the pocket conformation when the pocket is empty. However, the pocket was occupied by dioxane molecules from the crystallization solution. The pocket conformation was the same as that when it was occupied by the N-terminal arm, demonstrating that the pocket favors binding ligands of appropriate size and shape.

About this Structure

1WYK is a Single protein structure of sequence from Sindbis virus with and as ligands. Full crystallographic information is available from OCA.

Reference

Probing the potential glycoprotein binding site of sindbis virus capsid protein with dioxane and model building., Lee S, Kuhn RJ, Rossmann MG, Proteins. 1998 Nov 1;33(2):311-7. PMID:9779796

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