Structure of yellow fever virus envelope protein domain III
| Autor: | Alan D.T. Barrett, David E. Volk, Anjenique Anderson, David G. Gorenstein, Sai Hari A. Gandham, Jana J. von Lindern, Fiona J. May, David W.C. Beasley |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular viruses Molecular Sequence Data Protein domain Sequence alignment Biology Article Virus Neutralization 03 medical and health sciences Viral Envelope Proteins Viral envelope Virology Envelope protein domain III Humans Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Peptide sequence 030304 developmental biology 0303 health sciences Neutralization site 030306 microbiology Flavivirus Sequence Analysis DNA biology.organism_classification Molecular biology Protein Structure Tertiary 3. Good health Tissue tropism RNA Viral Yellow fever virus Sequence Alignment |
| Zdroj: | Virology. 394(1):12-18 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2009.09.001 |
| Popis: | The structure of recombinant domain III of the envelope protein (rED3) of yellow fever virus (YFV), containing the major neutralization site, was determined using NMR spectroscopy. The amino acid sequence and structure of the YFV-rED3 shows differences from ED3s of other mosquito-borne flaviviruses; in particular, the partially surface-exposed BC loop where methionine-304 and valine-324 were identified as being critical for the structure of the loop. Variations in the structure and surface chemistry of ED3 between flaviviruses affect neutralization sites and may affect host cell receptor interactions and play a role in the observed variations in viral pathogenesis and tissue tropism. |
| Databáze: | OpenAIRE |
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