1qqp

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spinqualitylabelsall models 1qqp, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.

Overview

Heparan sulfate has an important role in cell entry by foot-and-mouth, disease virus (FMDV). We find that subtype O1 FMDV binds this, glycosaminoglycan with a high affinity by immobilizing a specific highly, abundant motif of sulfated sugars. The binding site is a shallow, depression on the virion surface, located at the junction of the three, major capsid proteins, VP1, VP2 and VP3. Two pre-formed sulfate-binding, sites control receptor specificity. Residue 56 of VP3, an arginine in this, virus, is critical to this recognition, forming a key component of both, sites. This residue is a histidine in field isolates of the virus, switching to an arginine in adaptation to tissue culture, forming the high, affinity heparan sulfate-binding site. We postulate that this site is a, conserved feature of FMDVs, such that in the infected animal there is a, biological advantage to low affinity, or more selective, interactions with, glycosaminoglycan receptors.

About this Structure

1QQP is a Single protein structure of sequence from Foot-and-mouth disease virus. This structure superseeds the now removed PDB entry 1FHP. Full crystallographic information is available from OCA.

Reference

The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex., Fry EE, Lea SM, Jackson T, Newman JW, Ellard FM, Blakemore WE, Abu-Ghazaleh R, Samuel A, King AM, Stuart DI, EMBO J. 1999 Feb 1;18(3):543-54. PMID:9927414

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