Structure of simian virus 40 at 3.8-Å 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. Th...

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Bibliographic Details
Published in:Nature (London) 1991-11, Vol.354 (6351), p.278-284
Main Authors: Liddington, R. C, Yan, Y, Moulai, J, Sahli, R, Benjamin, T. L, Harrison, S. C
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biochemistry
Biological and medical sciences
Calcium-Binding Proteins - ultrastructure
Capsid - ultrastructure
Capsid Proteins
Computer Graphics
Crystallography
Disulfides - chemistry
Fundamental and applied biological sciences. Psychology
Humans
Macromolecular Substances
Microbiology
Models, Molecular
Molecular Sequence Data
Morphogenesis
Morphology, structure, chemical composition, physicochemical properties
Protein Conformation
Sequence Alignment
Simian virus 40 - ultrastructure
Virion - ultrastructure
Virology
Viruses
X-Ray Diffraction
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/354278a0