ABSTRACT
As mentioned before, the structure of the Bcl-2 family is monolithic and does not contain domains. It consists of two central hydrophobic helices, which are sur rounded by several amphipathic helices carrying the BH motifs. Of particular interest is a structure of the antiapoptotic Bcl-xL protein in complex with the BH3 motif of the proapoptotic Bax protein (Sattler et al., 1997). The interactions seen in this structure can explain the propensity of Bcl-2-like proteins to heterodimerize.
