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. 2008 Aug 21;105(34):12277–12282. doi: 10.1073/pnas.0711269105

Fig. 2.

Fig. 2.

Positively charged residues in Bcl-2 account for its tighter binding To ASPP2. (A) Sequence alignment of ASPP2 binding peptides: The ASPP2 binding peptides derived from the three Bcl proteins are bold and colored by amino acid type. (B and C) ELISA studies of ASPP2Ank-SH3 binding to Bcl-2 and Bcl-XL peptides modified at the nonconserved amino acid K15 and H18 of Bcl-2. (B) Peptides in which the positively charged residues from the Bcl-2 peptides were replaced by alanine or by the corresponding residues from Bcl-XL. (C) Peptides in which positive charges were introduced into the relevant positions at the Bcl-XL peptide.

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