Structure of simian virus 40 at 3.8-A resolution.
The crystallographically determined structure of simian virus 40 shows that the 72 pentamers of viral protein VP1, which form the outer shell, have identical conformations except for the C-terminal arms of their subunits. Five arms emerge from each pentamer and insert into neighbouring pentamers. This tying together of standard building blocks allows for the required variability in packing geometry without sacrificing specificity.
Liddington
R C
RC
Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138.
Yan
Y
Y
Moulai
J
J
Sahli
R
R
Benjamin
T L
TL
Harrison
S C
SC
D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000648:ultrastructure; D002213:Capsid / Q000648:ultrastructure*; D036022:Capsid Proteins; D003196:Computer Graphics; D003461:Crystallography; D004220:Disulfides / Q000737:chemistry; D006801:Humans; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009024:Morphogenesis; D011487:Protein Conformation; D016415:Sequence Alignment; D013539:Simian virus 40 / Q000648:ultrastructure*; D014771:Virion / Q000648:ultrastructure; D014961:X-Ray Diffraction
D002135:Calcium-Binding Proteins; D036022:Capsid Proteins; D004220:Disulfides; D046911:Macromolecular Substances; C062481:VP1 protein, polyomavirus