1d4b
From Proteopedia
(New page: 200px<br /> <applet load="1d4b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d4b" /> '''CIDE-N DOMAIN OF HUMAN CIDE-B'''<br /> ==O...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1d4b.gif|left|200px]]<br /> | + | [[Image:1d4b.gif|left|200px]]<br /><applet load="1d4b" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1d4b" size=" | + | |
caption="1d4b" /> | caption="1d4b" /> | ||
'''CIDE-N DOMAIN OF HUMAN CIDE-B'''<br /> | '''CIDE-N DOMAIN OF HUMAN CIDE-B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Apoptotic DNA fragmentation and chromatin condensation are mediated by the | + | 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== | ==About this Structure== | ||
| - | 1D4B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1D4B is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 22: | Line 21: | ||
[[Category: alpha/beta roll]] | [[Category: alpha/beta roll]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:49 2008'' |
Revision as of 10:12, 21 February 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 Thu Feb 21 12:12:49 2008
