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Figure 2.
Figure 2 Interhelical packing in IF[1]-H49K structure. (A)
Ribbon diagram of the active dimer. Dashed lines represent the
minimal inhibitory sequence. The disordered N-terminal residues
1 -18 are shown as dotted lines. (B) Schematic representation of
the interhelical packing. Residues involved in forming the
coiled coils are represented with their sequence number. Helices
are coloured as in Figure 1. Dotted lines represent the
continuity of the helices. The position of lysine 49 in helix C
(yellow) is shown in black, indicating the contacts with helices
B (sky blue) and D (dark blue). Dashed boxes show the two areas
of the protein represented in more detail in (C) and (D). (C)
Stereo view of the interhelical packing in the N-terminus of the
protein. (D) Stereo view of the interhelical packing in the
C-terminus of the AB dimer.
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