Publication Date:
1985-08-16
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, J W -- Silva, A M -- Murthy, M R -- Fita, I -- Rossmann, M G -- New York, N.Y. -- Science. 1985 Aug 16;229(4714):625-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023701" target="_blank"〉PubMed〈/a〉
Keywords:
Capsid/ultrastructure
;
Macromolecular Substances
;
Models, Molecular
;
Mosaic Viruses/*ultrastructure
;
Protein Binding
;
Protein Conformation
;
*Viral Proteins
;
X-Ray Diffraction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
