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Flavivirus capsid is a dimeric alpha-helical protein.
- Source :
-
Journal of virology [J Virol] 2003 Jun; Vol. 77 (12), pp. 7143-9. - Publication Year :
- 2003
-
Abstract
- The capsid proteins of two flaviviruses, yellow fever virus and dengue virus, were expressed in Escherichia coli and purified to near homogeneity suitable for biochemical characterization and structure determination by nuclear magnetic resonance. The oligomeric properties of the capsid protein in solution were investigated. In the absence of nucleic acid, both proteins were predominantly dimeric in solution. Further analysis of both proteins with far-UV circular dichroism spectroscopy indicated that they were largely alpha-helical. The secondary structure elements of the dengue virus capsid were determined by chemical shift indexing of the sequence-specific backbone resonance assignments. The dengue virus capsid protein devoid of its C-terminal signal sequence was found to be composed of four alpha helices. The longest alpha helix, 20 residues, is located at the C terminus and has an amphipathic character. In contrast, the N terminus was found to be unstructured and could be removed without disrupting the structural integrity of the protein.
- Subjects :
- Capsid metabolism
Capsid Proteins chemistry
Capsid Proteins genetics
Capsid Proteins metabolism
Circular Dichroism
Dengue Virus genetics
Dengue Virus metabolism
Dimerization
Escherichia coli genetics
Escherichia coli metabolism
Flavivirus chemistry
Flavivirus metabolism
Magnetic Resonance Spectroscopy
Protein Structure, Secondary
Yellow fever virus genetics
Yellow fever virus metabolism
Capsid chemistry
Dengue Virus chemistry
Yellow fever virus chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0022-538X
- Volume :
- 77
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Journal of virology
- Publication Type :
- Academic Journal
- Accession number :
- 12768036
- Full Text :
- https://doi.org/10.1128/jvi.77.12.7143-7149.2003