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Science 16 August 1985:
Vol. 229. no. 4714, pp. 625 - 629
DOI: 10.1126/science.4023701
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Articles

Science, Vol 229, Issue 4714, 625-629
Copyright © 1985 by American Association for the Advancement of Science

articles

The structure of a T = 1 icosahedral empty particle from southern bean mosaic virus

JW Erickson, AM Silva, MR Murthy, I Fita, and MG Rossmann

The structure of a T = 1 icosahedral particle (where T is the triangulation number), assembled from southern bean mosaic virus coat protein fragments that lacked the amino-terminal arm, was solved by means of model building procedures with the use of 6-angstrom resolution x-ray diffraction data. The icosahedral five-, three-, and twofold contacts were found to be similar, at this resolution, to the analogous contacts (icosahedral five-, quasi-three-, and quasi-twofolds) found in the parent T = 3 southern bean mosaic virus. However, the icosahedral fivefold contacts of the T = 3 structure are the most conserved in the T = 1 capsid. These results are consistent with a mechanism in which pentameric caps of dimers are the building blocks for the assembly of T = 1 and T = 3 icosahedral viruses.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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West Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody.
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Structural Requirements for the Assembly of Norwalk Virus-Like Particles.
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The three-dimensional structure of canine parvovirus and its functional implications.
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