1kqr
From Proteopedia
(New page: 200px<br /><applet load="1kqr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kqr, resolution 1.4Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1kqr.gif|left|200px]]<br /><applet load="1kqr" size=" | + | [[Image:1kqr.gif|left|200px]]<br /><applet load="1kqr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kqr, resolution 1.4Å" /> | caption="1kqr, resolution 1.4Å" /> | ||
'''Crystal Structure of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain in Complex with 2-O-methyl-alpha-D-N-acetyl neuraminic acid'''<br /> | '''Crystal Structure of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain in Complex with 2-O-methyl-alpha-D-N-acetyl neuraminic acid'''<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== | ||
| - | 1KQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhesus_rotavirus Rhesus rotavirus] with SO4, MNA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1KQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhesus_rotavirus Rhesus rotavirus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MNA:'>MNA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQR 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: GOL]] | [[Category: GOL]] | ||
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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 13:36:57 2008'' |
Revision as of 11:36, 21 February 2008
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Crystal Structure of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain in Complex with 2-O-methyl-alpha-D-N-acetyl neuraminic acid
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
1KQR is a Single protein structure of sequence from Rhesus rotavirus with , and as ligands. 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
Page seeded by OCA on Thu Feb 21 13:36:57 2008
Categories: Rhesus rotavirus | Single protein | Dormitzer, P R. | Harrison, S C. | Sun, Z Y.J. | Wagner, G. | GOL | MNA | SO4 | Cell attachment | Galectin fold | Hemagglutinin | Lectin | Neutralization antigen | Outer capsid | Rotavirus | Sialic acid | Spike protein | Vp4 | Vp8*
