Caspase-7 Variant 2 (V2) with reprogrammed substrate specificity due to Y230V/W232M/Q276C substitutions bound to VEID inhibitor.

Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition.

CASP-7,Apoptotic protease Mch-3,CMH-1,ICE-like apoptotic protease 3,ICE-LAP3

MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDK
VTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIK
DLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQAD

SGPINDTDANPRYKIPVEADFLFAYSTVPGYVSMRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESCSD
DPHFHEKKQIPCVVSMLTKELYFSQLEHHHHHH

300 mM diammonium citrate, 14% PEG 3350, 10 mM GuHCl, 20% glycerol

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Caspase-7 Y230A/W232M/S234N bound to DEVD inhibitor

Caspase-7 Y230A/W232M/S234N bound to VEID inhibitor

Caspase-7 wild-type bound to tetrapeptide inhibitor Ac-VEID-cho

Caspase-7 Y230V/W232M/Q276C bound to DEVD inhibitor

Caspase-7 Y230V/W232Y/S234V/Q276D bound to VEID inhibitor

Caspase-7 Y230V/W232Y/S234V/Q276D bound to DEVD inhibitor

wild-type caspase-7 bound to DEVD inhibitor

wild-type caspase-7 bound to LDESD inbibitor

Directed Evolution, Protease, Peptide Inhibitor, Designed Active Site Specificity, HYDROLASE-HYDROLASE INHIBITOR complex

SGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSD
DPHFHEKKQIPCVVSMLTKELYFSQ