1c9f
From Proteopedia
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| - | [[Image:1c9f.gif|left|200px]] | + | [[Image:1c9f.gif|left|200px]] |
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| - | '''NMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE''' | + | {{Structure |
| + | |PDB= 1c9f |SIZE=350|CAPTION= <scene name='initialview01'>1c9f</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C9F is a [ | + | 1C9F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The following page contains interesting information on the relation of 1C9F with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb56_1.html Caspases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9F OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the CAD domain of caspase-activated DNase and interaction with the CAD domain of its inhibitor., Uegaki K, Otomo T, Sakahira H, Shimizu M, Yumoto N, Kyogoku Y, Nagata S, Yamazaki T, J Mol Biol. 2000 Apr 14;297(5):1121-8. PMID:[http:// | + | Structure of the CAD domain of caspase-activated DNase and interaction with the CAD domain of its inhibitor., Uegaki K, Otomo T, Sakahira H, Shimizu M, Yumoto N, Kyogoku Y, Nagata S, Yamazaki T, J Mol Biol. 2000 Apr 14;297(5):1121-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10764577 10764577] |
[[Category: Caspases]] | [[Category: Caspases]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: alpha-beta roll]] | [[Category: alpha-beta roll]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:21:34 2008'' |
Revision as of 08:21, 20 March 2008
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NMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE
Overview
Caspase-activated DNase (CAD), which causes a genome fragmentation at the final stage of apoptosis, is a protein of about 40 kDa and exists as a complex form with the inhibitor ICAD in living cells. There is sequence homology of about 80 amino acid residues at the N termini of CAD and ICAD (called the CAD domain). Here, we report the three-dimensional structure of the CAD domain of CAD determined by multi-dimensional NMR spectroscopy and the property of CAD domains investigated by a surface plasmon resonance experiment. The CAD domain of CAD is an independently folded domain composed of one alpha-helix and five beta-strands forming a single sheet. The overall structure is categorized in the ubiquitin superfold. This domain can bind strongly to the isolated CAD domain of ICAD (dissociation constant: 5.48(+/-0.003)x10(-8) M). It suggests the function of the CAD domains in the CAD-ICAD system, that the protein-protein interaction through the CAD domains plays an important role in the inhibition of CAD DNase activity and in the correct folding of CAD. On the basis of structural comparison with other protein complexes containing the ubiquitin superfold, the interaction mode of the CAD domains is proposed.
About this Structure
1C9F is a Single protein structure of sequence from Mus musculus. The following page contains interesting information on the relation of 1C9F with [Caspases]. Full crystallographic information is available from OCA.
Reference
Structure of the CAD domain of caspase-activated DNase and interaction with the CAD domain of its inhibitor., Uegaki K, Otomo T, Sakahira H, Shimizu M, Yumoto N, Kyogoku Y, Nagata S, Yamazaki T, J Mol Biol. 2000 Apr 14;297(5):1121-8. PMID:10764577
Page seeded by OCA on Thu Mar 20 10:21:34 2008
