原创力文档vaccinia virus proteins a52 and b14 share a bcl-2–like fold but have evolved to inhibit nf-κb rather than apoptosis牛痘病毒蛋白质a52和b14 bcl-2-like褶皱但已进化到nf-κb而不是抑制细胞凋亡.pdfVIP
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vaccinia virus proteins a52 and b14 share a bcl-2–like fold but have evolved to inhibit nf-κb rather than apoptosis牛痘病毒蛋白质a52和b14 bcl-2-like褶皱但已进化到nf-κb而不是抑制细胞凋亡
Vaccinia Virus Proteins A52 and B14 Share a Bcl-2–Like
Fold but Have Evolved to Inhibit NF-kB rather than
Apoptosis
1. 1. 2. 2 1
Stephen C. Graham , Mohammad W. Bahar , Samantha Cooray , Ron A.-J. Chen , Daniel M. Whalen ,
1 1 1 1 2
Nicola G. A. Abrescia , David Alderton , Raymond J. Owens , David I. Stuart , Geoffrey L. Smith *,
Jonathan M. Grimes1*
1The Division of Structural Biology and the Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxfo rd, United Kingdom,
2 Department of Virology, Faculty of Medicine, Imperial College London, St. Mary’s Campus, London, United Kingdom
Abstract
Vaccinia virus (VACV), the prototype poxvirus, encodes numerous proteins that modulate the host response to infection.
Two such proteins, B14 and A52, act inside infected cells to inhibit activation of NF-kB, thereby blocking the production of
˚ ˚
pro-inflammatory cytokines. We have solved the crystal structures of A52 and B14 at 1.9 A and 2.7 A resolution, respectively.
Strikingly, both these proteins adopt a Bcl-2–like fold despite sharing no significant sequence similarity with other viral or
cellular Bcl-2–like proteins. Unlike cellular and viral Bcl-2–like proteins described previously, A52 and B14 lack a surface
groove for binding BH3 peptides from pro-apoptotic Bcl-2–like proteins and they do not modulate apoptosis. Structure-
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