National Laboratory of Protein Engineering and Plant Genetic Engineering

Laboratory of, China

National Laboratory of Protein Engineering and Plant Genetic Engineering

Laboratory of, China
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Wang X.-J.,National Laboratory of Protein Engineering and Plant Genetic Engineering | Cao Q.,National Laboratory of Protein Engineering and Plant Genetic Engineering | Liu X.,National Laboratory of Protein Engineering and Plant Genetic Engineering | Wang K.-T.,National Laboratory of Protein Engineering and Plant Genetic Engineering | And 6 more authors.
EMBO Reports | Year: 2010

Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N-Acetyl-Val-Glu-Ile-Asp-al-inhibited CASP6. Both of these forms of CASP6 have a dimeric structure, and in CASP6 zymogen the intersubunit cleavage site 190 TEVD 193 is well structured and inserts into the active site. This positions residue Asp 193 to be easily attacked by the catalytic residue Cys 163. We demonstrate biochemically that intramolecular cleavage at Asp 193 is a prerequisite for CASP6 self-activation and that this activation mechanism is dependent on the length of the L2 loop. Our results indicate that CASP6 can be activated and regulated through intramolecular self-cleavage. © 2010 European Molecular Biology Organization.

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