1i51: Difference between revisions
New page: left|200px<br /> <applet load="1i51" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i51, resolution 2.45Å" /> '''CRYSTAL STRUCTURE O... |
No edit summary |
||
| 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=" | |||
caption="1i51, resolution 2.45Å" /> | caption="1i51, resolution 2.45Å" /> | ||
'''CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP'''<br /> | '''CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP'''<br /> | ||
==Overview== | ==Overview== | ||
The inhibitor of apoptosis (IAP) proteins suppress cell death by | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==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:// | 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== | ==Reference== | ||
| Line 24: | Line 23: | ||
[[Category: protease]] | [[Category: protease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:06 2008'' | ||
Revision as of 14:08, 21 February 2008
|
CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Lymphoproliferative syndrome, X-linked, 2 OMIM:[300079]
About this StructureAbout this Structure
1I51 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of caspase-7 inhibition by XIAP., Chai J, Shiozaki E, Srinivasula SM, Wu Q, Datta P, Alnemri ES, Shi Y, Cell. 2001 Mar 9;104(5):769-80. PMID:11257230
Page seeded by OCA on Thu Feb 21 13:08:06 2008