1AR7
P1/MAHONEY POLIOVIRUS, DOUBLE MUTANT P1095S + H2142Y
Summary for 1AR7
| Entry DOI | 10.2210/pdb1ar7/pdb |
| Descriptor | P1/MAHONEY POLIOVIRUS, SPHINGOSINE, MYRISTIC ACID, ... (8 entities in total) |
| Functional Keywords | picornavirus, poliovirus, coat protein, icosahedral virus, virus |
| Biological source | Human poliovirus 1 More |
| Cellular location | Capsid protein VP0: Virion. Capsid protein VP4: Virion. Capsid protein VP2: Virion. Capsid protein VP3: Virion. Capsid protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 2C: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3A: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3AB: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Viral protein genome-linked: Virion. Protease 3C: Host cytoplasm. Protein 3CD: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P03300 P03300 P03300 |
| Total number of polymer chains | 5 |
| Total formula weight | 98485.19 |
| Authors | Wien, M.W.,Curry, S.,Filman, D.J.,Hogle, J.M. (deposition date: 1997-08-11, release date: 1997-12-03, Last modification date: 2024-11-13) |
| Primary citation | Wien, M.W.,Curry, S.,Filman, D.J.,Hogle, J.M. Structural studies of poliovirus mutants that overcome receptor defects. Nat.Struct.Biol., 4:666-674, 1997 Cited by PubMed Abstract: In order to better understand the process of cell entry for non-enveloped viruses, we have solved the crystal structures of five poliovirus mutants which can infect cells expressing mutant poliovirus receptors. Four of these structures have been solved from frozen crystals using cryocrystallographic data collection methods. The mutations have a range of structural consequences, from small local perturbations to significant loop rearrangements. All of the mutant viruses are more labile to conversion to an apparent cell entry intermediate, suggesting that these mutant viruses could compensate for the suboptimal receptors by lowering the thermal energy required to undergo the receptor-mediated conformational change. PubMed: 9253417DOI: 10.1038/nsb0897-666 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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