1KRI

NMR Solution Structures of the Rhesus Rotavirus VP4 Sialic Acid Binding Domain without Ligand

Summary for 1KRI

• Entry DOI: 10.2210/pdb1kri/pdb
• Related: 1KQR
• NMR Information: BMRB: 5275
• Descriptor: VP4 (1 entity in total)
• Functional Keywords: rotavirus, vp4, vp8*, spike protein, outer capsid, sialic acid, hemagglutinin, cell attachment, neutralization antigen, lectin, galectin fold, viral protein
• Biological source: Rhesus rotavirus
• Total number of polymer chains: 1
• Total formula weight: 20816.89

Authors

Dormitzer, P.R.,Sun, Z.-Y.J.,Wagner, G.,Harrison, S.C. (deposition date: 2002-01-09, release date: 2002-03-27, Last modification date: 2024-05-01)

Primary citation

Dormitzer, P.R.,Sun, Z.-Y.J.,Wagner, G.,Harrison, S.C.
The Rhesus Rotavirus VP4 Sialic Acid Binding Domain has a Galectin Fold with a Novel Carbohydrate Binding Site
Embo J., 21:885-897, 2002

PubMed Abstract: 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.

PubMed: 11867517
DOI: 10.1093/emboj/21.5.885

Experimental method

SOLUTION NMR