TY - JOUR
AU - Oh, B-H
AB - 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 (T
M) 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 T
M 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.
TI - Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions
JF - Cell Death & Differentiation
DO - 10.1038/sj.cdd.4401303
DA - 2003-08-01
UR - https://www.deepdyve.com/lp/springer-journals/unique-structural-features-of-a-bcl-2-family-protein-ced-9-and-3m4v2Y8r7z
SP - 1310
EP - 1319
VL - 10
IS - 12
DP - DeepDyve
ER -