1gfw

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(New page: 200px<br /> <applet load="1gfw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gfw, resolution 2.8&Aring;" /> '''THE 2.8 ANGSTROM CRY...)
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'''THE 2.8 ANGSTROM CRYSTAL STRUCTURE OF CASPASE-3 (APOPAIN OR CPP32)IN COMPLEX WITH AN ISATIN SULFONAMIDE INHIBITOR.'''<br />
'''THE 2.8 ANGSTROM CRYSTAL STRUCTURE OF CASPASE-3 (APOPAIN OR CPP32)IN COMPLEX WITH AN ISATIN SULFONAMIDE INHIBITOR.'''<br />
==Overview==
==Overview==
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Caspases have been strongly implicated to play an essential role in, apoptosis. A critical question regarding the role(s) of these proteases is, whether selective inhibition of an effector caspase(s) will prevent cell, death. We have identified potent and selective non-peptide inhibitors of, the effector caspases 3 and 7. The inhibition of apoptosis and maintenance, of cell functionality with a caspase 3/7-selective inhibitor is, demonstrated for the first time, and suggests that targeting these two, caspases alone is sufficient for blocking apoptosis. Furthermore, an x-ray, co-crystal structure of the complex between recombinant human caspase 3, and an isatin sulfonamide inhibitor has been solved to 2.8-A resolution., In contrast to previously reported peptide-based caspase inhibitors, the, isatin sulfonamides derive their selectivity for caspases 3 and 7 by, interacting primarily with the S(2) subsite, and do not bind in the, caspase primary aspartic acid binding pocket (S(1)). These inhibitors, blocked apoptosis in murine bone marrow neutrophils and human, chondrocytes. Furthermore, in camptothecin-induced chondrocyte apoptosis, cell functionality as measured by type II collagen promoter activity is, maintained, an activity considered essential for cartilage homeostasis., These data suggest that inhibiting chondrocyte cell death with a caspase, 3/7-selective inhibitor may provide a novel therapeutic approach for the, prevention and treatment of osteoarthritis, or other disease states, characterized by excessive apoptosis.
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Caspases have been strongly implicated to play an essential role in apoptosis. A critical question regarding the role(s) of these proteases is whether selective inhibition of an effector caspase(s) will prevent cell death. We have identified potent and selective non-peptide inhibitors of the effector caspases 3 and 7. The inhibition of apoptosis and maintenance of cell functionality with a caspase 3/7-selective inhibitor is demonstrated for the first time, and suggests that targeting these two caspases alone is sufficient for blocking apoptosis. Furthermore, an x-ray co-crystal structure of the complex between recombinant human caspase 3 and an isatin sulfonamide inhibitor has been solved to 2.8-A resolution. In contrast to previously reported peptide-based caspase inhibitors, the isatin sulfonamides derive their selectivity for caspases 3 and 7 by interacting primarily with the S(2) subsite, and do not bind in the caspase primary aspartic acid binding pocket (S(1)). These inhibitors blocked apoptosis in murine bone marrow neutrophils and human chondrocytes. Furthermore, in camptothecin-induced chondrocyte apoptosis, cell functionality as measured by type II collagen promoter activity is maintained, an activity considered essential for cartilage homeostasis. These data suggest that inhibiting chondrocyte cell death with a caspase 3/7-selective inhibitor may provide a novel therapeutic approach for the prevention and treatment of osteoarthritis, or other disease states characterized by excessive apoptosis.
==About this Structure==
==About this Structure==
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1GFW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MSI as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1QA8. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GFW OCA].
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1GFW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MSI:'>MSI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1QA8. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GFW OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Concha, N.O.]]
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[[Category: Concha, N O.]]
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[[Category: Janson, C.A.]]
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[[Category: Janson, C A.]]
[[Category: MSI]]
[[Category: MSI]]
[[Category: apopain]]
[[Category: apopain]]
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[[Category: x-ray]]
[[Category: x-ray]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:04:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:36 2008''

Revision as of 10:49, 21 February 2008


1gfw, resolution 2.8Å

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THE 2.8 ANGSTROM CRYSTAL STRUCTURE OF CASPASE-3 (APOPAIN OR CPP32)IN COMPLEX WITH AN ISATIN SULFONAMIDE INHIBITOR.

Overview

Caspases have been strongly implicated to play an essential role in apoptosis. A critical question regarding the role(s) of these proteases is whether selective inhibition of an effector caspase(s) will prevent cell death. We have identified potent and selective non-peptide inhibitors of the effector caspases 3 and 7. The inhibition of apoptosis and maintenance of cell functionality with a caspase 3/7-selective inhibitor is demonstrated for the first time, and suggests that targeting these two caspases alone is sufficient for blocking apoptosis. Furthermore, an x-ray co-crystal structure of the complex between recombinant human caspase 3 and an isatin sulfonamide inhibitor has been solved to 2.8-A resolution. In contrast to previously reported peptide-based caspase inhibitors, the isatin sulfonamides derive their selectivity for caspases 3 and 7 by interacting primarily with the S(2) subsite, and do not bind in the caspase primary aspartic acid binding pocket (S(1)). These inhibitors blocked apoptosis in murine bone marrow neutrophils and human chondrocytes. Furthermore, in camptothecin-induced chondrocyte apoptosis, cell functionality as measured by type II collagen promoter activity is maintained, an activity considered essential for cartilage homeostasis. These data suggest that inhibiting chondrocyte cell death with a caspase 3/7-selective inhibitor may provide a novel therapeutic approach for the prevention and treatment of osteoarthritis, or other disease states characterized by excessive apoptosis.

About this Structure

1GFW is a Protein complex structure of sequences from Homo sapiens with as ligand. This structure supersedes the now removed PDB entry 1QA8. Full crystallographic information is available from OCA.

Reference

Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality., Lee D, Long SA, Adams JL, Chan G, Vaidya KS, Francis TA, Kikly K, Winkler JD, Sung CM, Debouck C, Richardson S, Levy MA, DeWolf WE Jr, Keller PM, Tomaszek T, Head MS, Ryan MD, Haltiwanger RC, Liang PH, Janson CA, McDevitt PJ, Johanson K, Concha NO, Chan W, Abdel-Meguid SS, Badger AM, Lark MW, Nadeau DP, Suva LJ, Gowen M, Nuttall ME, J Biol Chem. 2000 May 26;275(21):16007-14. PMID:10821855

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