2PLV
STRUCTURAL FACTORS THAT CONTROL CONFORMATIONAL TRANSITIONS AND SEROTYPE SPECIFICITY IN TYPE 3 POLIOVIRUS
Summary for 2PLV
Entry DOI | 10.2210/pdb2plv/pdb |
Descriptor | HUMAN POLIOVIRUS TYPE 1 (SUBUNIT VP1), HUMAN POLIOVIRUS TYPE 1 (SUBUNIT VP2), HUMAN POLIOVIRUS TYPE 1 (SUBUNIT VP3), ... (7 entities in total) |
Functional Keywords | picornavirus, 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 P03300 |
Total number of polymer chains | 4 |
Total formula weight | 97920.64 |
Authors | Filman, D.J.,Hogle, J.M. (deposition date: 1989-10-17, release date: 1989-10-17, Last modification date: 2023-04-19) |
Primary citation | Filman, D.J.,Syed, R.,Chow, M.,Macadam, A.J.,Minor, P.D.,Hogle, J.M. Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus EMBO J., 8:1567-1579, 1989 Cited by PubMed Abstract: The three-dimensional structure of the Sabin strain of type 3 poliovirus has been determined at 2.4 A resolution. Significant structural differences with the Mahoney strain of type 1 poliovirus are confined to loops and terminal extensions of the capsid proteins, occur in all of the major antigenic sites of the virion and typically involve insertions, deletions or the replacement of prolines. Several newly identified components of the structure participate in assembly-dependent interactions which are relevant to the biologically important processes of viral assembly and uncoating. These include two sites of lipid substitution, two putative nucleotides and a beta sheet formed by the N-termini of capsid proteins VP4 and VP1. The structure provides an explanation for the temperature sensitive phenotype of the P3/Sabin strain. Amino acids that regulate temperature sensitivity in type 3 poliovirus are located in the interfaces between promoters, in the binding site for a lipid substituent and in an assembly-dependent extended beta sheet that stabilizes the association of pentamers. Several lines of evidence indicate that these structural components also control conformational transitions at various stages of the viral life cycle. PubMed: 2548847PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.88 Å) |
Structure validation
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