1kqr
From Proteopedia
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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''' | '''Crystal Structure of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain in Complex with 2-O-methyl-alpha-D-N-acetyl neuraminic acid''' | ||
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[[Category: Sun, Z Y.J.]] | [[Category: Sun, Z Y.J.]] | ||
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
| - | [[Category: | + | [[Category: Cell attachment]] |
| - | [[Category: | + | [[Category: Galectin fold]] |
| - | [[Category: | + | [[Category: Hemagglutinin]] |
| - | [[Category: | + | [[Category: Lectin]] |
| - | [[Category: | + | [[Category: Neutralization antigen]] |
| - | [[Category: | + | [[Category: Outer capsid]] |
| - | [[Category: | + | [[Category: Rotavirus]] |
| - | [[Category: | + | [[Category: Sialic acid]] |
| - | [[Category: | + | [[Category: Spike protein]] |
| - | [[Category: | + | [[Category: Vp4]] |
| - | [[Category: | + | [[Category: Vp8*]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:03:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:03, 2 May 2008
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. 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 Fri May 2 23:03:37 2008
