1i51: Difference between revisions

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[[Image:1i51.gif|left|200px]]<br />

[[Image:1i51.gif|left|200px]]<br /><applet load="1i51" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1i51" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1i51, resolution 2.45Å" />

'''CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP'''<br />

==Overview==

The inhibitor of apoptosis (IAP) proteins suppress cell death by, inhibiting the catalytic activity of caspases. Here we present the crystal, structure of caspase-7 in complex with a potent inhibitory fragment from, XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic, groove of caspase-7, making extensive contacts to the residues that are, essential for its catalytic activity. Strikingly, despite a reversal of, relative orientation, a subset of interactions between caspase-7 and XIAP, closely resemble those between caspase-7 and its tetrapeptide inhibitor, DEVD-CHO. Our biochemical and structural analyses reveal that the BIR, domains are dispensable for the inhibition of caspase-3 and -7. This study, provides a structural basis for the design of the next-generation caspase, inhibitors.

The inhibitor of apoptosis (IAP) proteins suppress cell death by inhibiting the catalytic activity of caspases. Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic groove of caspase-7, making extensive contacts to the residues that are essential for its catalytic activity. Strikingly, despite a reversal of relative orientation, a subset of interactions between caspase-7 and XIAP closely resemble those between caspase-7 and its tetrapeptide inhibitor DEVD-CHO. Our biochemical and structural analyses reveal that the BIR domains are dispensable for the inhibition of caspase-3 and -7. This study provides a structural basis for the design of the next-generation caspase inhibitors.

==Disease==

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==About this Structure==

1I51 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1I51 OCA].

1I51 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1I51 OCA].

==Reference==

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[[Category: protease]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 17~~:26:~~26 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:06 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1i51.gif|left|200px]]<br />
+[[Image:1i51.gif|left|200px]]<br /><applet load="1i51" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1i51" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1i51, resolution 2.45&Aring;" />
 '''CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP'''<br />
 ==Overview==
-The inhibitor of apoptosis (IAP) proteins suppress cell death by, inhibiting the catalytic activity of caspases. Here we present the crystal, structure of caspase-7 in complex with a potent inhibitory fragment from, XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic, groove of caspase-7, making extensive contacts to the residues that are, essential for its catalytic activity. Strikingly, despite a reversal of, relative orientation, a subset of interactions between caspase-7 and XIAP, closely resemble those between caspase-7 and its tetrapeptide inhibitor, DEVD-CHO. Our biochemical and structural analyses reveal that the BIR, domains are dispensable for the inhibition of caspase-3 and -7. This study, provides a structural basis for the design of the next-generation caspase, inhibitors.
+The inhibitor of apoptosis (IAP) proteins suppress cell death by inhibiting the catalytic activity of caspases. Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic groove of caspase-7, making extensive contacts to the residues that are essential for its catalytic activity. Strikingly, despite a reversal of relative orientation, a subset of interactions between caspase-7 and XIAP closely resemble those between caspase-7 and its tetrapeptide inhibitor DEVD-CHO. Our biochemical and structural analyses reveal that the BIR domains are dispensable for the inhibition of caspase-3 and -7. This study provides a structural basis for the design of the next-generation caspase inhibitors.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-I51 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1I51 OCA].
+I51 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1I51 OCA].
 ==Reference==
@@ Line 24: / Line 23: @@
 [[Category: protease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:26:26 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:06 2008''