Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions

J. S. Woo, J. S. Jung, N. C. Ha, J. Shin, K. H. Kim, W. Lee, B. H. Oh

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33 Citations (Scopus)


The interactions between B-cell lymphoma 2 (BCL-2) family members are known to be mediated through the binding of the BH3 domain of a proapoptotic member to the BH3-binding groove of an antiapoptotic member. We determined the crystal structure of antiapoptotic CED-9, which reveals a unique C-terminal helix altering the common BH3-binding region. A coexpression system to produce CED-9 in complex with proapoptotic EGL-1 enabled us to show that the binding of EGL-1 to CED-9 is extremely stable, raising the melting temperature (Tm) of CED-9 by 25°C, and that the binding surface of CED-9 extends beyond the BH3-binding region and reaches the BH4 domain. Consistently, the Tm and a 1H-15N correlation NMR spectrum of CED-9 in complex with EGL-1 are drastically different from those of CED-9 in complex with the EGL-1 BH3 peptide. The data suggest that the recognition between other BCL-2 family members may also involve much wider protein surfaces than is previously thought.

Original languageEnglish
Pages (from-to)1310-1319
Number of pages10
JournalCell Death and Differentiation
Issue number12
Publication statusPublished - 2003 Dec 1


All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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