1DGI
Cryo-EM structure of human poliovirus(serotype 1)complexed with three domain CD155
Summary for 1DGI
| Entry DOI | 10.2210/pdb1dgi/pdb |
| Related | 1BIH 1CIC 1NEU 2PLV |
| Descriptor | POLIOVIRUS RECEPTOR, VP1, VP2, ... (5 entities in total) |
| Functional Keywords | cd155, pvr, human poliovirus, poliovirus-receptor complex, icosahedral virus, virus-receptor complex, virus/receptor |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 127686.07 |
| Authors | He, Y.,Bowman, V.D.,Mueller, S.,Bator, C.M.,Bella, J.,Peng, X.,Baker, T.S.,Wimmer, E.,Kuhn, R.J.,Rossmann, M.G. (deposition date: 1999-11-24, release date: 2000-01-24, Last modification date: 2024-02-07) |
| Primary citation | He, Y.,Bowman, V.D.,Mueller, S.,Bator, C.M.,Bella, J.,Peng, X.,Baker, T.S.,Wimmer, E.,Kuhn, R.J.,Rossmann, M.G. Interaction of the poliovirus receptor with poliovirus. Proc.Natl.Acad.Sci.USA, 97:79-84, 2000 Cited by PubMed Abstract: The structure of the extracellular, three-domain poliovirus receptor (CD155) complexed with poliovirus (serotype 1) has been determined to 22-A resolution by means of cryo-electron microscopy and three-dimensional image-reconstruction techniques. Density corresponding to the receptor was isolated in a difference electron density map and fitted with known structures, homologous to those of the three individual CD155 Ig-like domains. The fit was confirmed by the location of carbohydrate moieties in the CD155 glycoprotein, the conserved properties of elbow angles in the structures of cell surface molecules with Ig-like folds, and the concordance with prior results of CD155 and poliovirus mutagenesis. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. However, the orientation of the long, slender CD155 molecule relative to the poliovirus surface is quite different from the orientation of intercellular adhesion molecule-1 on rhinoviruses. In addition, the residues that provide specificity of recognition differ for the two receptors. The principal feature of receptor binding common to these two picornaviruses is the site in the canyon at which binding occurs. This site may be a trigger for initiation of the subsequent uncoating step required for viral infection. PubMed: 10618374DOI: 10.1073/pnas.97.1.79 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (22 Å) |
Structure validation
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