1D4B

CIDE-N DOMAIN OF HUMAN CIDE-B

Summary for 1D4B

• Entry DOI: 10.2210/pdb1d4b/pdb
• NMR Information: BMRB: 4574
• Descriptor: HUMAN CELL DEATH-INDUCING EFFECTOR B (1 entity in total)
• Functional Keywords: alpha/beta roll, apoptosis
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 13748.54

Authors

Lugovskoy, A.,Zhou, P.,Chou, J.,McCarty, J.,Li, P.,Wagner, G. (deposition date: 1999-10-02, release date: 1999-12-17, Last modification date: 2024-05-22)

Primary citation

Lugovskoy, A.A.,Zhou, P.,Chou, J.J.,McCarty, J.S.,Li, P.,Wagner, G.
Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE-N/CIDE-N interactions in the DNA fragmentation pathway of apoptosis.
Cell(Cambridge,Mass.), 99:747-755, 1999

PubMed Abstract: Apoptotic DNA fragmentation and chromatin condensation are mediated by the caspase-activated DFF40/ CAD nuclease, which is chaperoned and inhibited by DFF45/ICAD. CIDE proteins share a homologous regulatory CIDE-N domain with DFF40/CAD and DFF45/ ICAD. Here we report the solution structure of CIDE-N of human CIDE-B. We show that the CIDE-N of CIDE-B interacts with CIDE-N domains of both DFF40 and DFF45. The binding epitopes are similar and map to a highly charged bipolar surface region of CIDE-B. Furthermore, we demonstrate that the CIDE-N of CIDE-B regulates enzymatic activity of the DFF40/ DFF45 complex in vitro. Based on these results and mutagenesis data, we propose a model for the CIDE-N/ CIDE-N complex and discuss the role of this novel bipolar interaction in mediating downstream events of apoptosis.

PubMed: 10619428
DOI: 10.1016/S0092-8674(00)81672-4

Experimental method

SOLUTION NMR