1d4b
From Proteopedia
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'''CIDE-N DOMAIN OF HUMAN CIDE-B''' | '''CIDE-N DOMAIN OF HUMAN CIDE-B''' | ||
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[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
[[Category: Zhou, P.]] | [[Category: Zhou, P.]] | ||
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Revision as of 10:26, 2 May 2008
CIDE-N DOMAIN OF HUMAN CIDE-B
Overview
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.
About this Structure
1D4B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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., Lugovskoy AA, Zhou P, Chou JJ, McCarty JS, Li P, Wagner G, Cell. 1999 Dec 23;99(7):747-55. PMID:10619428 Page seeded by OCA on Fri May 2 13:26:07 2008
