3EPC
CryoEM structure of poliovirus receptor bound to poliovirus type 1
3EPC の概要
エントリーDOI | 10.2210/pdb3epc/pdb |
関連するPDBエントリー | 3EOW 3EPD 3EPF |
EMDBエントリー | 1570 |
分子名称 | Poliovirus receptor, Protein VP1, Protein VP2, ... (7 entities in total) |
機能のキーワード | cd155 structure immunoglobulin superfamily, poliovirus capsid jelly role, cell adhesion, cell membrane, glycoprotein, host-virus interaction, immunoglobulin domain, membrane, receptor, secreted, transmembrane, viral protein, virus |
由来する生物種 | Homo sapiens (human) 詳細 |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 118606.19 |
構造登録者 | Zhang, P.,Mueller, S.,Morais, M.C.,Bator, C.M.,Bowman, V.D.,Hafenstein, S.,Wimmer, E.,Rossmann, M.G. (登録日: 2008-09-29, 公開日: 2008-11-11, 最終更新日: 2024-10-09) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (8 Å) |
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