2cjy
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Caspases are cysteine proteases involved in the signalling cascades of, programmed cell death in which caspase-3 plays a central role, since it, propagates death signals from intrinsic and extrinsic stimuli to, downstream targets. The atomic resolution (1.06 Angstroms) crystal, structure of the caspase-3 DEVD-cmk complex reveals the structural basis, for substrate selectivity in the S4 pocket. A low-barrier hydrogen bond is, observed between the side-chains of the P4 inhibitor aspartic acid and, Asp179 of the N-terminal tail of the symmetry related p12 subunit., Site-directed mutagenesis of Asp179 confirmed the significance of this, residue in substrate recognition. In the 1.06 Angstroms crystal structure, a radiation damage induced rearrangement of the inhibitor methylketone, moiety was .. | + | Caspases are cysteine proteases involved in the signalling cascades of, programmed cell death in which caspase-3 plays a central role, since it, propagates death signals from intrinsic and extrinsic stimuli to, downstream targets. The atomic resolution (1.06 Angstroms) crystal, structure of the caspase-3 DEVD-cmk complex reveals the structural basis, for substrate selectivity in the S4 pocket. A low-barrier hydrogen bond is, observed between the side-chains of the P4 inhibitor aspartic acid and, Asp179 of the N-terminal tail of the symmetry related p12 subunit., Site-directed mutagenesis of Asp179 confirmed the significance of this, residue in substrate recognition. In the 1.06 Angstroms crystal structure, a radiation damage induced rearrangement of the inhibitor methylketone, moiety was observed. The carbon atom that in a substrate would represent, the scissile peptide bond carbonyl carbon clearly shows a tetrahedral, coordination and resembles the postulated tetrahedral intermediate of the, acylation reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 2CJY is a | + | 2CJY 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 PHQ as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CJY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:56:06 2007'' |
Revision as of 12:50, 5 November 2007
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EXTENDED SUBSTRATE RECOGNITION IN CASPASE-3 REVEALED BY HIGH RESOLUTION X-RAY STRUCTURE ANALYSIS
Overview
Caspases are cysteine proteases involved in the signalling cascades of, programmed cell death in which caspase-3 plays a central role, since it, propagates death signals from intrinsic and extrinsic stimuli to, downstream targets. The atomic resolution (1.06 Angstroms) crystal, structure of the caspase-3 DEVD-cmk complex reveals the structural basis, for substrate selectivity in the S4 pocket. A low-barrier hydrogen bond is, observed between the side-chains of the P4 inhibitor aspartic acid and, Asp179 of the N-terminal tail of the symmetry related p12 subunit., Site-directed mutagenesis of Asp179 confirmed the significance of this, residue in substrate recognition. In the 1.06 Angstroms crystal structure, a radiation damage induced rearrangement of the inhibitor methylketone, moiety was observed. The carbon atom that in a substrate would represent, the scissile peptide bond carbonyl carbon clearly shows a tetrahedral, coordination and resembles the postulated tetrahedral intermediate of the, acylation reaction.
About this Structure
2CJY is a Protein complex structure of sequences from Homo sapiens with PHQ as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis., Ganesan R, Mittl PR, Jelakovic S, Grutter MG, J Mol Biol. 2006 Jun 23;359(5):1378-88. Epub 2006 May 11. PMID:16787777
Page seeded by OCA on Mon Nov 5 14:56:06 2007
Categories: Homo sapiens | Protein complex | Ganesan, R. | Grutter, M.G. | Jelakovic, S. | Mittl, P.R.E. | PHQ | Apoptosis | Clan cd | Complex (hydrolase-inhibitor) | Complex (protease-inhibitor) | Cpp32 | Cysteine-protease | Hydrolase | Ice | Phosphorylation | Polymorphism | Protease | Safety catch | Tetramer | Thiol protease | Yama | Zymogen
