A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members.

@article{Diaz1997ACB,
  title={A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members.},
  author={J L Diaz and Tillman Oltersdorf and William Horne and Melanie Jane McConnell and Gary G Wilson and Stephen Weeks and Tsai Garcia and Lawrence C. Fritz},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 17},
  pages={11350-5}
}
Bcl-2 inhibits apoptosis induced by a wide variety of stimuli. In contrast, the Bcl-2 homologue, Bax, antagonizes Bcl-2's death protecting function. Bcl-2 forms protein-protein homodimers with itself and heterodimers with Bax, and previous experiments have shown that point mutations in Bcl-2 can abrogate Bax binding while leaving homodimerization intact. These mutagenesis results can be interpreted to suggest that Bcl-2 has separate binding sites that are responsible for homodimer and… CONTINUE READING

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