NMR determination that an extended BH3 motif of pro-apoptotic BID is specifically bound to BCL-XL.
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.
Ji
Hong
H
The New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027-7556, USA.
Shekhtman
Alex
A
Ghose
Ranajeet
R
McDonnell
James M
JM
Cowburn
David
D
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D051023:BH3 Interacting Domain Death Agonist Protein / Q000737:chemistry* / Q000235:genetics; D005453:Fluorescence; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D051028:bcl-2-Associated X Protein / Q000737:chemistry* / Q000235:genetics
D051023:BH3 Interacting Domain Death Agonist Protein; D051028:bcl-2-Associated X Protein