| Autor: |
van Roon AM; Biophysical Structural Chemistry, Leiden Institute of Chemistry, P.O. Box 9502, 2300 RA Leiden, The Netherlands., Bink HH, Plaisier JR, Pleij CW, Abrahams JP, Pannu NS |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of molecular biology [J Mol Biol] 2004 Aug 27; Vol. 341 (5), pp. 1205-14. |
| DOI: |
10.1016/j.jmb.2004.06.085 |
| Abstrakt: |
Empty capsids (artificial top component) of turnip yellow mosaic virus were co-crystallized with an encapsidation initiator RNA hairpin. No clear density was observed for the RNA, but there were clear differences in the conformation of a loop of the coat protein at the opening of the pentameric capsomer (formed by five A-subunits) protruding from the capsid, compared to the corresponding loop in the intact virus. Further differences were found at the N terminus of the A-subunit. These differences have implications for the mechanism of decapsidation of the virus, required for infection. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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