2cjy
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2cjy |SIZE=350|CAPTION= <scene name='initialview01'>2cjy</scene>, resolution 1.67Å | |PDB= 2cjy |SIZE=350|CAPTION= <scene name='initialview01'>2cjy</scene>, resolution 1.67Å | ||
|SITE= <scene name='pdbsite=AC1:Phq+Binding+Site+For+Chain+I'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Phq+Binding+Site+For+Chain+I'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=PHQ:FORMIC ACID BENZYL ESTER'>PHQ</scene> | + | |LIGAND= <scene name='pdbligand=ASK:DEHYDROXYMETHYLASPARTIC+ACID'>ASK</scene>, <scene name='pdbligand=PHQ:FORMIC+ACID+BENZYL+ESTER'>PHQ</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjy OCA], [http://www.ebi.ac.uk/pdbsum/2cjy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cjy RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Jelakovic, S.]] | [[Category: Jelakovic, S.]] | ||
[[Category: Mittl, P R.E.]] | [[Category: Mittl, P R.E.]] | ||
| - | [[Category: PHQ]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: clan cd]] | [[Category: clan cd]] | ||
| Line 44: | Line 46: | ||
[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:33 2008'' |
Revision as of 23:22, 30 March 2008
| |||||||
| , resolution 1.67Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 31 02:22:33 2008
Categories: Homo sapiens | Protein complex | Ganesan, R. | Grutter, M G. | Jelakovic, S. | Mittl, P R.E. | Apoptosis | Clan cd | Complex (hydrolase-inhibitor) | Complex (protease-inhibitor) | Cpp32 | Cysteine-protease | Hydrolase | Ice | Phosphorylation | Polymorphism | Protease | Safety catch | Tetramer | Thiol protease | Yama | Zymogen
