Abstract
The ebolaviruses can cause severe hemorrhagic fever. Essential to the ebolavirus life cycle is the protein VP30, which serves as a transcriptional cofactor. Here, the crystal structure of the C-terminal, NP-binding domain of VP30 from Reston ebolavirus is presented. Reston VP30 and Ebola VP30 both form homodimers, but the dimeric interfaces are rotated relative to each other, suggesting subtle inherent differences or flexibility in the dimeric interface.
Keywords:
Please provide keywords.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallization
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Crystallography, X-Ray
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Ebolavirus / chemistry*
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Ebolavirus / classification
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Ebolavirus / metabolism
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Protein Structure, Tertiary
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Sequence Homology, Amino Acid
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Transcription Factors / chemistry*
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Transcription Factors / genetics
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Transcription Factors / metabolism
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Viral Proteins / chemistry*
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Viral Proteins / genetics
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Viral Proteins / metabolism
Substances
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Transcription Factors
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VP30 protein, ebola virus
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Viral Proteins