Abstract
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.
Original language | English (US) |
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Pages (from-to) | S101-S107 |
Journal | Magnetic Resonance in Chemistry |
Volume | 44 |
Issue number | 7 SPEC. ISS. |
DOIs | |
State | Published - Jul 2006 |
Keywords
- Apoptosis
- BCL-X
- BH3 motif
- BID
- C
- Death agonist
- H
- Helical propensity
- N
- NMR
ASJC Scopus subject areas
- Chemistry(all)
- Materials Science(all)