1kri
From Proteopedia
(New page: 200px<br /><applet load="1kri" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kri" /> '''NMR Solution Structures of the Rhesus Rotavi...) |
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| - | [[Image:1kri.gif|left|200px]]<br /><applet load="1kri" size=" | + | [[Image:1kri.gif|left|200px]]<br /><applet load="1kri" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR Solution Structures of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain without Ligand'''<br /> | '''NMR Solution Structures of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain without Ligand'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cell attachment and membrane penetration are functions of the rotavirus | + | Cell attachment and membrane penetration are functions of the rotavirus outer capsid spike protein, VP4. An activating tryptic cleavage of VP4 produces the N-terminal fragment, VP8*, which is the viral hemagglutinin and an important target of neutralizing antibodies. We have determined, by X-ray crystallography, the atomic structure of the VP8* core bound to sialic acid and, by NMR spectroscopy, the structure of the unliganded VP8* core. The domain has the beta-sandwich fold of the galectins, a family of sugar binding proteins. The surface corresponding to the galectin carbohydrate binding site is blocked, and rotavirus VP8* instead binds sialic acid in a shallow groove between its two beta-sheets. There appears to be a small induced fit on binding. The residues that contact sialic acid are conserved in sialic acid-dependent rotavirus strains. Neutralization escape mutations are widely distributed over the VP8* surface and cluster in four epitopes. From the fit of the VP8* core into the virion spikes, we propose that VP4 arose from the insertion of a host carbohydrate binding domain into a viral membrane interaction protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1KRI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhesus_rotavirus Rhesus rotavirus]. Full crystallographic information is available from [http:// | + | 1KRI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhesus_rotavirus Rhesus rotavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rhesus rotavirus]] | [[Category: Rhesus rotavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dormitzer, P | + | [[Category: Dormitzer, P R.]] |
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
| - | [[Category: Sun, Z | + | [[Category: Sun, Z Y.J.]] |
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
[[Category: cell attachment]] | [[Category: cell attachment]] | ||
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[[Category: vp8*]] | [[Category: vp8*]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:10 2008'' |
Revision as of 11:37, 21 February 2008
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NMR Solution Structures of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain without Ligand
Overview
Cell attachment and membrane penetration are functions of the rotavirus outer capsid spike protein, VP4. An activating tryptic cleavage of VP4 produces the N-terminal fragment, VP8*, which is the viral hemagglutinin and an important target of neutralizing antibodies. We have determined, by X-ray crystallography, the atomic structure of the VP8* core bound to sialic acid and, by NMR spectroscopy, the structure of the unliganded VP8* core. The domain has the beta-sandwich fold of the galectins, a family of sugar binding proteins. The surface corresponding to the galectin carbohydrate binding site is blocked, and rotavirus VP8* instead binds sialic acid in a shallow groove between its two beta-sheets. There appears to be a small induced fit on binding. The residues that contact sialic acid are conserved in sialic acid-dependent rotavirus strains. Neutralization escape mutations are widely distributed over the VP8* surface and cluster in four epitopes. From the fit of the VP8* core into the virion spikes, we propose that VP4 arose from the insertion of a host carbohydrate binding domain into a viral membrane interaction protein.
About this Structure
1KRI is a Single protein structure of sequence from Rhesus rotavirus. Full crystallographic information is available from OCA.
Reference
The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site., Dormitzer PR, Sun ZY, Wagner G, Harrison SC, EMBO J. 2002 Mar 1;21(5):885-97. PMID:11867517
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