1kqr

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{{STRUCTURE_1kqr| PDB=1kqr | SCENE= }}
{{STRUCTURE_1kqr| PDB=1kqr | SCENE= }}
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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'''
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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===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11867517 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11867517}}
==About this Structure==
==About this Structure==
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[[Category: Vp4]]
[[Category: Vp4]]
[[Category: Vp8*]]
[[Category: Vp8*]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:03:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:47:34 2008''

Revision as of 07:47, 2 July 2008

Template:STRUCTURE 1kqr

Crystal Structure of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain in Complex with 2-O-methyl-alpha-D-N-acetyl neuraminic acid

Template:ABSTRACT PUBMED 11867517

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

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