Autor: |
H A, AL-Khayat, D, Bhella, J M, Kenney, J F, Roth, A J, Kingsman, E, Martin-Rendon, H R, Saibil |
Rok vydání: |
1999 |
Předmět: |
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Zdroj: |
Journal of molecular biology. 292(1) |
ISSN: |
0022-2836 |
Popis: |
The virus-like particles (VLPs) produced by the yeast Ty retrotransposons are structurally and functionally related to retroviral cores. Using cryo-electron microscopy (cryo-EM) and three-dimensional (3D) reconstruction, we have examined the structures of VLPs assembled from full-length and truncated forms of the capsid structural protein. The VLPs are highly polydisperse in their radius distribution. We have found that the length of the C-terminal region of the capsid structural protein dictates the T -number, and thus the size, of the assembled particles. Each construct studied appears to assemble into at least two or three size classes, with shorter C termini giving rise to smaller particles. This assembly property provides a model for understanding the variable assembly of retroviral core proteins. The particles are assembled from trimer-clustered units and there are holes in the capsid shells. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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