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NMR determination that an extended BH3 motif of pro‐apoptotic BID is specifically bound to BCL‐X L
Author(s) -
Ji Hong,
Shekhtman Alex,
Ghose Ranajeet,
McDonnell James M.,
Cowburn David
Publication year - 2006
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1856
Subject(s) - chemistry , motif (music) , apoptosis , cytochrome c , cleavage (geology) , intramolecular force , microbiology and biotechnology , mitochondrion , caspase 3 , stereochemistry , programmed cell death , biochemistry , biology , physics , fracture (geology) , acoustics , paleontology
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 . Copyright © 2006 John Wiley & Sons, Ltd.