3crd: Difference between revisions

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[[Image:3crd.gif|left|200px]]<br />

[[Image:3crd.gif|left|200px]]<br /><applet load="3crd" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="3crd" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="3crd" />

'''NMR STRUCTURE OF THE RAIDD CARD DOMAIN, 15 STRUCTURES'''<br />

==Overview==

Apoptosis requires recruitment of caspases by receptor-associated adaptors, through homophilic interactions between the CARDs (caspase recruitment, domains) of adaptor proteins and prodomains of caspases. We have solved, the CARD structure of the RAIDD adaptor protein that recruits, ICH-1/caspase-2. It consists of six tightly packed helices arranged in a, topology homologous to the Fas death domain. The surface contains a basic, and an acidic patch on opposite sides. This polarity is conserved in the, ICH-1 CARD as indicated by homology modeling. Mutagenesis data suggest, that these patches mediate CARD/CARD interaction between RAIDD and ICH-1., Subsequent modeling of the CARDs of Apaf-1 and caspase-9, as well as Ced-4, and Ced-3, showed that the basic/acidic surface polarity is highly, conserved, suggesting a general mode for CARD/CARD interaction.

Apoptosis requires recruitment of caspases by receptor-associated adaptors through homophilic interactions between the CARDs (caspase recruitment domains) of adaptor proteins and prodomains of caspases. We have solved the CARD structure of the RAIDD adaptor protein that recruits ICH-1/caspase-2. It consists of six tightly packed helices arranged in a topology homologous to the Fas death domain. The surface contains a basic and an acidic patch on opposite sides. This polarity is conserved in the ICH-1 CARD as indicated by homology modeling. Mutagenesis data suggest that these patches mediate CARD/CARD interaction between RAIDD and ICH-1. Subsequent modeling of the CARDs of Apaf-1 and caspase-9, as well as Ced-4 and Ced-3, showed that the basic/acidic surface polarity is highly conserved, suggesting a general mode for CARD/CARD interaction.

==About this Structure==

3CRD 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=3CRD OCA].

3CRD 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=3CRD OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Chou, J.J.]]

[[Category: Chou, J J.]]

[[Category: Duan, H.]]

[[Category: Matsuo, H.]]

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[[Category: homophilic interaction]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:55 2008''

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@@ Line 1: / Line 1: @@
-[[Image:3crd.gif|left|200px]]<br />
+[[Image:3crd.gif|left|200px]]<br /><applet load="3crd" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="3crd" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="3crd" />
 '''NMR STRUCTURE OF THE RAIDD CARD DOMAIN, 15 STRUCTURES'''<br />
 ==Overview==
-Apoptosis requires recruitment of caspases by receptor-associated adaptors, through homophilic interactions between the CARDs (caspase recruitment, domains) of adaptor proteins and prodomains of caspases. We have solved, the CARD structure of the RAIDD adaptor protein that recruits, ICH-1/caspase-2. It consists of six tightly packed helices arranged in a, topology homologous to the Fas death domain. The surface contains a basic, and an acidic patch on opposite sides. This polarity is conserved in the, ICH-1 CARD as indicated by homology modeling. Mutagenesis data suggest, that these patches mediate CARD/CARD interaction between RAIDD and ICH-1., Subsequent modeling of the CARDs of Apaf-1 and caspase-9, as well as Ced-4, and Ced-3, showed that the basic/acidic surface polarity is highly, conserved, suggesting a general mode for CARD/CARD interaction.
+Apoptosis requires recruitment of caspases by receptor-associated adaptors through homophilic interactions between the CARDs (caspase recruitment domains) of adaptor proteins and prodomains of caspases. We have solved the CARD structure of the RAIDD adaptor protein that recruits ICH-1/caspase-2. It consists of six tightly packed helices arranged in a topology homologous to the Fas death domain. The surface contains a basic and an acidic patch on opposite sides. This polarity is conserved in the ICH-1 CARD as indicated by homology modeling. Mutagenesis data suggest that these patches mediate CARD/CARD interaction between RAIDD and ICH-1. Subsequent modeling of the CARDs of Apaf-1 and caspase-9, as well as Ced-4 and Ced-3, showed that the basic/acidic surface polarity is highly conserved, suggesting a general mode for CARD/CARD interaction.
 ==About this Structure==
-CRD 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=3CRD OCA].
+CRD 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=3CRD OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Chou, J.J.]]
+[[Category: Chou, J J.]]
 [[Category: Duan, H.]]
 [[Category: Matsuo, H.]]
@@ Line 22: / Line 21: @@
 [[Category: homophilic interaction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:47:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:55 2008''