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Figure 2.
Fig. 2. Comparison of putative transmembrane regions. (A)
Cartoon diagrams of domains d3 of C8  -MACPF (left) and
intermedilysin (right). The putative ß hairpin regions
ß1-ß2 and TMH1 are colored in dark brown, and
ß3-ß4 and TMH2 are colored in light brown. (B)
Sequence alignment of (i) the ß1-ß2 and
ß3-ß4 regions of C8 , C9, and
perforin (Perf) and (ii) TMH1 and TMH2 of perfringolysin (PFO)
and intermedilysin (ILY). Residues (31) are colored according to
character: hydrophobic (green), positively charged (blue),
negatively charged (red), and hydrophilic (white). Yellow
indicates cysteine residues. Secondary structure elements, as
observed for C8 -MACPF and
intermedilysin, are indicated. Putative transmembrane regions
are indicated by gray boxes.
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