Caspase-6

Basic Information
Short Name	CASP6
UNP ID	P55212
Organism	Homo sapiens
Cys Site	Cys163
Family/Domain	Peptidase C14A family
Known Ligand	Ligand list
Function Type	Protease

Summary

Protein Function

Caspase-6 is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases-7, -8 and -10, and is thought to function as a downstream enzyme in the caspase activation cascade.

Caspase-6 can also undergo self-processing without other members of the caspase family. Alternative splicing of this gene results in two transcript variants that encode different isoforms. (From Wikipedia)

Cys Function & Property

The catalytic triad in Caspase-6 comprises Cys163, His121 and Arg64.

• Hydrophobic property:

• SASA:

Cys163: 60.255 A^2

Protein Sequence

MSSASGLRRG HPAGGEENMT ETDAFYKREM FDPAEKYKMD HRRRGIALIF
NHERFFWHLT LPERRGTCAD RDNLTRRFSD LGFEVKCFND LKAEELLLKI
HEVSTVSHAD ADCFVCVFLS HGEGNHIYAY DAKIEIQTLT GLFKGDKCHS
LVGKPKIFII QACRGNQHDV PVIPLDVVDN QTEKLDTNIT EVDAASVYTL
PAGADFLMCY SVAEGYYSHR ETVNGSWYIQ DLCEMLGKYG SSLEFTELLT
LVNRKVSQRR VDFCKDPSAI GKKQVPCFAS MLTKKLHFFP KSN

Structural Information

• Known structure with covalent ligand:
  

3P4U

3QNW

3S70

• Protein structure:

Related Pathway

• Apoptosis
  

Experimental Evidence

Crystallography, Site-directed mutation assasy

Reference

1. Müller I, Lamers M B A C, Ritchie A J, et al. Structure of human caspase-6 in complex with Z-VAD-FMK: new peptide binding mode observed for the non-canonical caspase conformation[J]. Bioorganic & medicinal chemistry letters, 2011, 21(18): 5244-5247. 21820899
   
2. Liu X, Zhang H, Wang X J, et al. Get phases from arsenic anomalous scattering: de novo SAD phasing of two protein structures crystallized in cacodylate buffer[J]. PLoS One, 2011, 6(9): e24227. 21912678