Abstract
Poxviruses encode immuno-modulatory proteins capable of subverting host defenses. The poxvirus vaccinia expresses a small 14-kDa protein, N1L, that is critical for virulence. We report the crystal structure of N1L, which reveals an unexpected but striking resemblance to host apoptotic regulators of the B cell lymphoma-2 (Bcl-2) family. Although N1L lacks detectable Bcl-2 homology (BH) motifs at the sequence level, we show that N1L binds with high affinity to the BH3 peptides of pro-apoptotic Bcl-2 family proteins in vitro, consistent with a role for N1L in modulating host antiviral defenses.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Crystallography, X-Ray
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Dimerization
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Hydrophobic and Hydrophilic Interactions
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In Vitro Techniques
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Models, Molecular
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Molecular Sequence Data
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Protein Binding
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Protein Conformation
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Protein Structure, Quaternary
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Proto-Oncogene Proteins c-bcl-2 / chemistry
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Proto-Oncogene Proteins c-bcl-2 / genetics
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Sequence Homology, Amino Acid
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Vaccinia virus / chemistry*
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Vaccinia virus / genetics
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Viral Proteins / chemistry*
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Viral Proteins / genetics
Substances
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N1L protein, Vaccinia virus
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Proto-Oncogene Proteins c-bcl-2
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Viral Proteins