2o71: Difference between revisions

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[[Image:2o71.gif|left|200px]]<br />

[[Image:2o71.gif|left|200px]]<br /><applet load="2o71" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2o71" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2o71, resolution 2.0Å" />

'''Crystal structure of RAIDD DD'''<br />

==Overview==

Caspase-2 is implicated in stress-induced apoptosis that acts as an, upstream initiator of mitochondrial permeabilization. Recent studies have, shown that caspase-2 activation requires a molecular complex known as the, PIDDosome comprising the p53-inducible protein PIDD, the adapter protein, RAIDD and caspase-2. RAIDD has an N-terminal caspase recruitment domain, (CARD) that interacts with the CARD of caspase-2 and a C-terminal death, domain (DD) that interacts with the DD in PIDD. As a first step towards, elucidating the molecular mechanisms of caspase-2 activation, we report, the crystal structure of RAIDD DD at 2.0 A resolution. The high-resolution, structure reveals important features of RAIDD DD that may be important for, DD folding and dynamics and for assembly of the PIDDosome.

Caspase-2 is implicated in stress-induced apoptosis that acts as an upstream initiator of mitochondrial permeabilization. Recent studies have shown that caspase-2 activation requires a molecular complex known as the PIDDosome comprising the p53-inducible protein PIDD, the adapter protein RAIDD and caspase-2. RAIDD has an N-terminal caspase recruitment domain (CARD) that interacts with the CARD of caspase-2 and a C-terminal death domain (DD) that interacts with the DD in PIDD. As a first step towards elucidating the molecular mechanisms of caspase-2 activation, we report the crystal structure of RAIDD DD at 2.0 A resolution. The high-resolution structure reveals important features of RAIDD DD that may be important for DD folding and dynamics and for assembly of the PIDDosome.

==About this Structure==

2O71 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2O71 OCA].

2O71 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=2O71 OCA].

==Reference==

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[[Category: raidd]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 23~~:07:~~16 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:15:12 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2o71.gif|left|200px]]<br />
+[[Image:2o71.gif|left|200px]]<br /><applet load="2o71" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2o71" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2o71, resolution 2.0&Aring;" />
 '''Crystal structure of RAIDD DD'''<br />
 ==Overview==
-Caspase-2 is implicated in stress-induced apoptosis that acts as an, upstream initiator of mitochondrial permeabilization. Recent studies have, shown that caspase-2 activation requires a molecular complex known as the, PIDDosome comprising the p53-inducible protein PIDD, the adapter protein, RAIDD and caspase-2. RAIDD has an N-terminal caspase recruitment domain, (CARD) that interacts with the CARD of caspase-2 and a C-terminal death, domain (DD) that interacts with the DD in PIDD. As a first step towards, elucidating the molecular mechanisms of caspase-2 activation, we report, the crystal structure of RAIDD DD at 2.0 A resolution. The high-resolution, structure reveals important features of RAIDD DD that may be important for, DD folding and dynamics and for assembly of the PIDDosome.
+Caspase-2 is implicated in stress-induced apoptosis that acts as an upstream initiator of mitochondrial permeabilization. Recent studies have shown that caspase-2 activation requires a molecular complex known as the PIDDosome comprising the p53-inducible protein PIDD, the adapter protein RAIDD and caspase-2. RAIDD has an N-terminal caspase recruitment domain (CARD) that interacts with the CARD of caspase-2 and a C-terminal death domain (DD) that interacts with the DD in PIDD. As a first step towards elucidating the molecular mechanisms of caspase-2 activation, we report the crystal structure of RAIDD DD at 2.0 A resolution. The high-resolution structure reveals important features of RAIDD DD that may be important for DD folding and dynamics and for assembly of the PIDDosome.
 ==About this Structure==
-O71 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2O71 OCA].
+O71 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=2O71 OCA].
 ==Reference==
@@ Line 19: / Line 18: @@
 [[Category: raidd]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:07:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:15:12 2008''