1d4b
From Proteopedia
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| - | [[Image:1d4b.gif|left|200px]] | + | [[Image:1d4b.gif|left|200px]] |
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| - | '''CIDE-N DOMAIN OF HUMAN CIDE-B''' | + | {{Structure |
| + | |PDB= 1d4b |SIZE=350|CAPTION= <scene name='initialview01'>1d4b</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CIDE-N DOMAIN OF HUMAN CIDE-B''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1D4B is a [ | + | 1D4B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4B OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10619428 10619428] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha/beta roll]] | [[Category: alpha/beta roll]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:32:40 2008'' |
Revision as of 08:32, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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