核磁共振测定表明，促凋亡蛋白BID的一个延伸BH3基序与BCL-XL特异性结合。
NMR determination that an extended BH3 motif of pro-apoptotic BID is specifically bound to BCL-XL.
作者信息
Ji Hong, Shekhtman Alex, Ghose Ranajeet, McDonnell James M, Cowburn David
机构信息
The New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027-7556, USA.
出版信息
Magn Reson Chem. 2006 Jul;44 Spec No(Spec No):S101-7. doi: 10.1002/mrc.1856.
The BH3 motif of the pro-survival family of proteins, BCL, is also present in pro-apoptotic proteins like BID and BAX. Homo- and hetero-oligomerization interactions of the BH3 motif are generally recognized as the critical component of their apoptotic activities. In full-length BID, the putative hydrophobic binding surface of its BH3 motif is substantially occluded by intramolecular contacts, many of which are removed on BID's transformation to tBID by cleavage with caspase 8, required for tBID's pro-apoptotic action on mitochondria, thereby releasing cytochrome c.
促生存蛋白家族BCL的BH3基序也存在于诸如BID和BAX等促凋亡蛋白中。BH3基序的同源和异源寡聚化相互作用通常被认为是其凋亡活性的关键组成部分。在全长BID中，其BH3基序假定的疏水结合表面基本上被分子内接触所遮蔽，其中许多在BID被半胱天冬酶8切割转化为tBID时被去除，这是tBID对线粒体促凋亡作用所必需的，从而释放细胞色素c。
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