Structural and enzymatic insights into caspase-2 protein substrate recognition and catalysis.

MQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQE
KLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQD

GKEKLPKMRLPTRSDMICGYACLKGTAAMRNAKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHR
CKEMSEYCSTLCRHLYLFPGHPPTLEHHHHHH

0.1M HEPES, 15% PEG 3350, 3mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

caspase-2 bound with two copies of Ac-DVAD-CHO

caspase-2 bound to one copy of Ac-DVAD-CHO

crystal structure of active caspase-2 bound with Ac-VDVAD-CHO

crystal structure of active caspase-2 bound with Ac-ADVAD-CHO

THERE ARE NO LINKS BETWEEN CYS 320 AND CHAINS E,F

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Caspase-2 subunit p18 (E.C.3.4.22.-), Caspase-2 subunit p12 (E.C.3.4.22.-), Peptide Inhibitor (ACE)VDVAD-CHO

hydrolase, apoptosis, HYDROLASE-HYDROLASE INHIBITOR complex

QVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEK
LQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQD

GKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHR
CKEMSEYCSTLCRHLYLFPGHPPT

BINDING SITE FOR CHAIN E OF PEPTIDE (ACE)VDVAD-CHO

BINDING SITE FOR CHAIN F OF PEPTIDE (ACE)VDVAD-CHO