Vaccinia Virus Proteins A52 and B14 Share a Bcl-2–Like Fold but Have Evolved to Inhibit NF-κB rather than Apoptosis
Figure 2
A52, B14 and N1 utilise a conserved face for dimerisation, but the 2-fold rotations that relate monomers of the dimers differ significantly.
(A) Superposition of A52 (orange), B14 (magenta) and N1 (cyan; PDB ID 2uxe). (B–D) The molecular surfaces of (B) A52, (C) B14 and (D) N1 are shown in white, residues that form intermolecular (dimer) contacts being coloured orange (A52), magenta (B14) or cyan (N1). The molecules are oriented as in (A). Cylinders represent the two-fold rotation axes of the respective dimers.