1OHU

Structure of Caenorhabditis elegans CED-9

Summary for 1OHU

• Entry DOI: 10.2210/pdb1ohu/pdb
• Descriptor: APOPTOSIS REGULATOR CED-9 (2 entities in total)
• Functional Keywords: apoptosis, ced-9, bcl-2 family
• Biological source: CAENORHABDITIS ELEGANS
• Cellular location: Endomembrane system; Peripheral membrane protein: P41958
• Total number of polymer chains: 2
• Total formula weight: 41626.32

Authors

Jeong, J.-S.,Ha, N.-C.,Oh, B.-H. (deposition date: 2003-05-31, release date: 2003-08-14, Last modification date: 2024-11-13)

Primary citation

Woo, J.-S.,Jung, J.-S.,Ha, N.-C.,Shin, J.,Kim, K.-H.,Lee, W.,Oh, B.-H.
Unique Structural Features of a Bcl-2 Family Protein Ced-9 and Biophysical Characterization of Ced-9/Egl-1 Interactions
Cell Death Differ., 10:1310-, 2003

PubMed Abstract: 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 degrees 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.

PubMed: 12894216
DOI: 10.1038/SJ.CDD.4401303

Experimental method

X-RAY DIFFRACTION (2.03 Å)