Skip to main content
. 2009 Mar 6;5(3):e1000330. doi: 10.1371/journal.ppat.1000330

Figure 1. The tetramer interface of A2 and sequence alignment with A3G.

Figure 1

(A) Detail of the A2 tetramer interface, highlighting residues that mediate oligomerization interactions. One subunit is shown in blue (left) and one in orange (right). Residues F155 and W157 are shown in blue, other residues from the left-hand subunit that contribute interactions are shown in yellow, and residues from the right-hand subunit are in green; all are indicated by labels. (B) Sequence alignment of A2 with the A3G N- and C-CDA domains corresponding to the L1 loop of A2. Arrows indicate the position of β-strands, and a barrel indicates the position of an α-helix in the A2 crystal structure. Below the alignment, residues in A3G are indicated that correspond to F155 and W157 in A2.