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PMID: 1659663 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Structure of simian virus 40 at 3.8-A resolution.

Nature ·Vol. 354 ·No. 6351 ·1991-11-28 ·Pages 278-84

Liddington RC, Yan Y, Moulai J, Sahli R, Benjamin TL, Harrison SC

Abstract

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.

MeSH Terms

Amino Acid Sequence Calcium-Binding Proteins/ultrastructure Capsid/ultrastructure Capsid Proteins Computer Graphics Crystallography Disulfides/chemistry Humans Macromolecular Substances Models, Molecular Molecular Sequence Data Morphogenesis Protein Conformation Sequence Alignment Simian virus 40/ultrastructure Virion/ultrastructure X-Ray Diffraction

Chemicals

Calcium-Binding Proteins Capsid Proteins Disulfides Macromolecular Substances VP1 protein, polyomavirus

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Liddington R C

Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138.

Yan Y

Moulai J

Sahli R

Benjamin T L

Harrison S C

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/354278a0

Published

1991-11-28

Pages

278-84

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/354278a0 View journal details

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Structure of simian virus 40 at 3.8-A resolution.

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