Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 105, Issue 47, Page 18284-18289, Year 2008
Publish date	Nov 25, 2008
Authors	Ping Zhang / Steffen Mueller / Marc C Morais / Carol M Bator / Valorie D Bowman / Susan Hafenstein / Eckard Wimmer / Michael G Rossmann /
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 ...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.
External links	Proc Natl Acad Sci U S A / PubMed:19011098 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	3.5005 - 9.0 Å
Structure data	1562 3epd EMDB-1562: CryoEM reconstructions of PV3 complexed with deglycosylated CD155 PDB-3epd: CryoEM structure of poliovirus receptor bound to poliovirus type 3 Method: EM (single particle) / Resolution: 9.0 Å 1563 3epf EMDB-1563: CryoEM reconstructions of PV2 complexed with deglycosylated CD155 PDB-3epf: CryoEM structure of poliovirus receptor bound to poliovirus type 2 Method: EM (single particle) / Resolution: 9.0 Å 1570 3epc EMDB-1570: CryoEM reconstructions of PV1 complexed with deglycosylated CD155 PDB-3epc: CryoEM structure of poliovirus receptor bound to poliovirus type 1 Method: EM (single particle) / Resolution: 8.0 Å PDB-3uro: Poliovirus receptor CD155 D1D2 Method: X-RAY DIFFRACTION / Resolution: 3.5005 Å
Chemicals	ChemComp-SPH: SPHINGOSINE / Sphingosine ChemComp-MYR: MYRISTIC ACID / Myristic acid ChemComp-SC4: 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE ChemComp-HOH: WATER / Water
Source	homo sapiens (human) human poliovirus 1 mahoney human poliovirus 3 poliovirus type 2
Keywords	VIRUS / CD155 structure Immunoglobulin Superfamily / poliovirus capsid jelly role / Cell adhesion / Cell membrane / Glycoprotein / Host-virus interaction / Immunoglobulin domain / Membrane / Receptor / Secreted / Transmembrane / VIRAL PROTEIN / poliovirus receptor ectodomain / Immunoglobulin Super Family