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West Nile virus core protein; tetramer structure and ribbon formation
- Source :
- Structure (London, England : 1993)
- Publication Year :
- 2004
-
Abstract
- We have determined the crystal structure of the core (C) protein from the Kunjin subtype of West Nile virus (WNV), closely related to the NY99 strain of WNV, currently a major health threat in the U.S. WNV is a member of the Flaviviridae family of enveloped RNA viruses that contains many important human pathogens. The C protein is associated with the RNA genome and forms the internal core which is surrounded by the envelope in the virion. The C protein structure contains four alpha helices and forms dimers that are organized into tetramers. The tetramers form extended filamentous ribbons resembling the stacked alpha helices seen in HEAT protein structures.
- Subjects :
- Viral protein
viruses
Viral Core Proteins
Molecular Sequence Data
virus diseases
RNA
Biology
Dengue virus
biology.organism_classification
medicine.disease_cause
Crystallography, X-Ray
Virology
Article
Protein Structure, Secondary
Flaviviridae
Protein structure
Capsid
Structural Biology
medicine
Amino Acid Sequence
Protein Structure, Quaternary
Molecular Biology
Peptide sequence
West Nile virus
Alpha helix
Subjects
Details
- ISSN :
- 09692126
- Volume :
- 12
- Issue :
- 7
- Database :
- OpenAIRE
- Journal :
- Structure (London, England : 1993)
- Accession number :
- edsair.doi.dedup.....300a21550fe63595b31277b8d619b9b2