Summary for 3URO
| Entry DOI | 10.2210/pdb3uro/pdb |
| Related | 3EPC 3EPD 3EPF |
| Descriptor | Poliovirus receptor (1 entity in total) |
| Functional Keywords | poliovirus receptor ectodomain, immunoglobulin super family, cell adhesion, cell membrane, glycoprotein, host-virus interaction, immunoglobulin domain, membrane, receptor, secreted, transmembrane, viral protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 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 |
| Total number of polymer chains | 1 |
| Total formula weight | 24355.65 |
| Authors | Zhang, P.,Mueller, S.,Morais, M.C.,Bator, C.M.,Bowman, V.D.,Hafenstein, S.,Wimmer, E.,Rossmann, M.G. (deposition date: 2011-11-22, release date: 2011-12-07) |
| Primary citation | Zhang, P.,Mueller, S.,Morais, M.C.,Bator, C.M.,Bowman, V.D.,Hafenstein, S.,Wimmer, E.,Rossmann, M.G. Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses. Proc.Natl.Acad.Sci.USA, 105:18284-18289, 2008 Cited by PubMed Abstract: When poliovirus (PV) recognizes its receptor, CD155, the virus changes from a 160S to a 135S particle before releasing its genome into the cytoplasm. CD155 is a transmembrane protein with 3 Ig-like extracellular domains, D1-D3, where D1 is recognized by the virus. The crystal structure of D1D2 has been determined to 3.5-A resolution and fitted into approximately 8.5-A resolution cryoelectron microscopy reconstructions of the virus-receptor complexes for the 3 PV serotypes. These structures show that, compared with human rhinoviruses, the virus-receptor interactions for PVs have a greater dependence on hydrophobic interactions, as might be required for a virus that can inhabit environments of different pH. The pocket factor was shown to remain in the virus during the first recognition stage. The present structures, when combined with earlier mutational investigations, show that in the subsequent entry stage the receptor moves further into the canyon when at a physiological temperature, thereby expelling the pocket factor and separating the viral subunits to form 135S particles. These results provide a detailed analysis of how a nonenveloped virus can enter its host cell. PubMed: 19011098DOI: 10.1073/pnas.0807848105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5005 Å) |
Structure validation
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