1d4b: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4b OCA], [http://www.ebi.ac.uk/pdbsum/1d4b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d4b RCSB]</span> | |||
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[[Category: alpha/beta roll]] | [[Category: alpha/beta roll]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:34:25 2008'' | ||
Revision as of 19:34, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CIDE-N DOMAIN OF HUMAN CIDE-B
OverviewOverview
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 StructureAbout this Structure
1D4B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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