1kke
From Proteopedia
(New page: 200px<br /><applet load="1kke" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kke, resolution 2.6Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1kke.gif|left|200px]]<br /><applet load="1kke" size=" | + | [[Image:1kke.gif|left|200px]]<br /><applet load="1kke" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kke, resolution 2.6Å" /> | caption="1kke, resolution 2.6Å" /> | ||
'''Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer'''<br /> | '''Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Reovirus attaches to cellular receptors with the sigma1 protein, a | + | Reovirus attaches to cellular receptors with the sigma1 protein, a fiber-like molecule protruding from the 12 vertices of the icosahedral virion. The crystal structure of a receptor-binding fragment of sigma1 reveals an elongated trimer with two domains: a compact head with a new beta-barrel fold and a fibrous tail containing a triple beta-spiral. Numerous structural and functional similarities between reovirus sigma1 and the adenovirus fiber suggest an evolutionary link in the receptor-binding strategies of these two viruses. A prominent loop in the sigma1 head contains a cluster of residues that are conserved among reovirus serotypes and are likely to form a binding site for junction adhesion molecule, an integral tight junction protein that serves as a reovirus receptor. The fibrous tail is mainly responsible for sigma1 trimer formation, and it contains a highly flexible region that allows for significant movement between the base of the tail and the head. The architecture of the trimer interface and the observed flexibility indicate that sigma1 is a metastable structure poised to undergo conformational changes upon viral attachment and cell entry. |
==About this Structure== | ==About this Structure== | ||
| - | 1KKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.]. Full crystallographic information is available from [http:// | + | 1KKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Reovirus sp.]] | [[Category: Reovirus sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chappell, J | + | [[Category: Chappell, J D.]] |
| - | [[Category: Dermody, T | + | [[Category: Dermody, T S.]] |
| - | [[Category: Prota, A | + | [[Category: Prota, A E.]] |
[[Category: Stehle, T.]] | [[Category: Stehle, T.]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
| Line 25: | Line 25: | ||
[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:07 2008'' |
Revision as of 11:35, 21 February 2008
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Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer
Overview
Reovirus attaches to cellular receptors with the sigma1 protein, a fiber-like molecule protruding from the 12 vertices of the icosahedral virion. The crystal structure of a receptor-binding fragment of sigma1 reveals an elongated trimer with two domains: a compact head with a new beta-barrel fold and a fibrous tail containing a triple beta-spiral. Numerous structural and functional similarities between reovirus sigma1 and the adenovirus fiber suggest an evolutionary link in the receptor-binding strategies of these two viruses. A prominent loop in the sigma1 head contains a cluster of residues that are conserved among reovirus serotypes and are likely to form a binding site for junction adhesion molecule, an integral tight junction protein that serves as a reovirus receptor. The fibrous tail is mainly responsible for sigma1 trimer formation, and it contains a highly flexible region that allows for significant movement between the base of the tail and the head. The architecture of the trimer interface and the observed flexibility indicate that sigma1 is a metastable structure poised to undergo conformational changes upon viral attachment and cell entry.
About this Structure
1KKE is a Single protein structure of sequence from Reovirus sp.. Full crystallographic information is available from OCA.
Reference
Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber., Chappell JD, Prota AE, Dermody TS, Stehle T, EMBO J. 2002 Jan 15;21(1-2):1-11. PMID:11782420
Page seeded by OCA on Thu Feb 21 13:35:07 2008
Categories: Reovirus sp. | Single protein | Chappell, J D. | Dermody, T S. | Prota, A E. | Stehle, T. | Beta-barrel | Beta-spiral | Fiber | Receptor-binding | Reovirus | Sigma1 | Trimer
