Figure 3
Conserved interactions and structural motifs in the Bcl-B:Bim interface. (a) Molecular details of two highly conserved polar interactions in the BH1 motif of Bcl-2 proteins. A helix capping motif is formed between the acceptor atom of the side chain of the first residue preceding helix α5 (T83) and the donor amide proton of R86.30 Shown is also the ionic interaction between R86 of Bcl-B and D67 of Bim (represented yellow) and the α4–α5 loop residue D78 of Bcl-B. (b) The hydrophobic pocket of Bcl-B enclosing the conserved L62 of Bim. Residues within 4 Å of Bim L62 are labeled. (c) Bcl-B sequences bear a conserved ionic interaction between Asp15 and Arg40 located on α1 and α2 of Bcl-B, respectively
