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Figure 5.
FIG. 5. The ribbon representations of the structures of
BCL-w (P117V) (a), BAX (b), and BCL-x[L]/BAK-BH3-peptide complex
(c). Odd numbered helices are blue, and even numbered helices
are green. The C-terminal -helices in BCL-w and
BAX proteins and the bound peptide in the BCL-x[L] complex are
red. d presents a view of the BCL-w binding cleft and bound
C-terminal helix. Helix 8 and its hydrophobic
residues are shown in green. The cleft surface is blue, red, and
yellow to show positive (Arg, Lys, His), negative (Asp, Glu),
and hydrophobic (Val, Leu, Ile, Ala, Phe, Tyr, Trp) residues,
respectively. Other residue types are gray.
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