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学术论文
Qi SQ, Pang YX, Hu Q, Liu Q, Li H, Zhou YL, He TX, Liang QL, Liu YX, Yuan XQ2, Luo GA, Li HL, Wang JW, Yan N#, Shi YG#. Crystal Structure of the Caenorhabditis elegans Apoptosome Reveals an Octameric Assembly of CED-4. CELL 141:446-457, 2009 ( # indicates corresponding authors).
发布时间:2011-11-16作者:颜宁关键字:

Abstract
The CED-4 homo-oligomer or apoptosome is required for initiation of programmed cell death in Caenorhabditis elegans by facilitating autocatalytic activation of the CED-3 caspase zymogen. How the CED-4 apoptosome assembles and activates CED-3 remains enigmatic. Here we report the crystal structure of the complete CED-4 apoptosome and show that it consists of eight CED-4 molecules, organized as a tetramer of an asymmetric dimer via a previously unreported interface among AAA(+) ATPases. These eight CED-4 molecules form a funnel-shaped structure. The mature CED-3 protease is monomeric in solution and forms an active holoenzyme with the CED-4 apoptosome, within which the protease activity of CED-3 is markedly stimulated. Unexpectedly, the octameric CED-4 apoptosome appears to bind only two, not eight, molecules of mature CED-3. The structure of the CED-4 apoptosome reveals shared principles for the NB-ARC family of AAA(+) ATPases and suggests a mechanism for the activation of CED-3.




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