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1NN8

CryoEM structure of poliovirus receptor bound to poliovirus

Summary for 1NN8
Entry DOI10.2210/pdb1nn8/pdb
Related1DGI
Descriptorpoliovirus receptor, coat protein VP1, coat protein VP2, ... (6 entities in total)
Functional Keywordsicosahedral virus, picornavirus, virus-receptor complex, virus/receptor
Biological sourceHomo sapiens (human)
More
Cellular locationIsoform Alpha: Cell membrane; Single-pass type I membrane protein. Isoform Delta: Cell membrane; Single-pass type I membrane protein. Isoform Beta: Secreted. Isoform Gamma: Secreted: P15151
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: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P03300 P03300 P03300 P03300
Total number of polymer chains7
Total formula weight196051.10
Authors
He, Y.,Mueller, S.,Chipman, P.R.,Bator, C.M.,Peng, X.,Bowman, V.D.,Mukhopadhyay, S.,Wimmer, E.,Kuhn, R.J.,Rossmann, M.G. (deposition date: 2003-01-13, release date: 2004-01-27, Last modification date: 2024-02-14)
Primary citationHe, Y.,Mueller, S.,Chipman, P.R.,Bator, C.M.,Peng, X.,BOWMAN, V.D.,MUKHOPADHYAY, S.,Wimmer, E.,Kuhn, R.J.,Rossmann, M.G.
Complexes of poliovirus serotypes with their common cellular receptor, CD155
J.Virol., 77:4827-4835, 2003
Cited by
PubMed Abstract: Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy. Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry. Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface. The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155. The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating. In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating. The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization. Many of these are likely to have lost their ability to bind CD155, resulting in there being only three PV serotypes.
PubMed: 12663789
DOI: 10.1128/JVI.77.8.4827-4835.2003
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (15 Å)
Structure validation

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数据于2025-07-09公开中

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