Fig. 5: Binding mode of 35 to Bcl-2-xL.

a Ribbon diagram of the structure of the Bcl-2-xL/35 complex with the lowest NOE energy with the Bcl-2-xL ribbon in blue and 35 represented by stick models (carbon atoms in yellow, nitrogen atoms in blue, oxygen atoms in red and bromine atoms in pink). The positions of the N- and C-termini are labeled N and C, respectively, and the eight α-helices are labeled α1-α8. The position of residue 165, which corresponds to residue 206 of native Bcl-2, is indicated. b Close-up view of the 35 binding site with Bcl-2-xL represented by a cyan ribbon and stick models (carbon atoms in cyan, nitrogen atoms in blue, oxygen atoms in red and sulfur atoms in light orange). Selected Bcl-2-xL side chains that contact 35 are labeled. c, d Close up view of the 35 binding site with the molecular surface of Bcl-2-xL shown in blue and 35 represented by stick models. In (d), the surface of the juxtamembrane region at the C-terminus of Bcl-2-xL was removed such that the binding site of 35 on the globular domain can be observed.