Summary for 1QQP
| Entry DOI | 10.2210/pdb1qqp/pdb |
| Descriptor | PROTEIN (GENOME POLYPROTEIN), 2-O-sulfo-alpha-L-gulopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-gulopyranuronic acid, ... (6 entities in total) |
| Functional Keywords | virus, heparan sulphate, virus-receptor interactions/protein-carbohydrate interactions, virus/viral protein, icosahedral virus |
| Biological source | Foot-and-mouth disease virus More |
| Cellular location | Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B-1: Virion (Potential). Protein 3B-2: Virion (Potential). Protein 3B-3: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P03305 P03305 P03305 P03305 |
| Total number of polymer chains | 4 |
| Total formula weight | 82269.74 |
| Authors | Fry, E.E.,Lea, S.M.,Jackson, T.,Newman, J.W.I.,Ellard, F.M.,Blakemore, W.E.,Abu-Ghazaleh, R.,Samuel, A.,King, A.M.Q.,Stuart, D.I. (deposition date: 1999-05-20, release date: 1999-06-18, Last modification date: 2024-11-13) |
| Primary citation | Fry, E.E.,Lea, S.M.,Jackson, T.,Newman, J.W.,Ellard, F.M.,Blakemore, W.E.,Abu-Ghazaleh, R.,Samuel, A.,King, A.M.,Stuart, D.I. The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex. EMBO J., 18:543-554, 1999 Cited by PubMed Abstract: 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. PubMed: 9927414DOI: 10.1093/emboj/18.3.543 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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