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Photocontrolled Exposure of Pro‐apoptotic Peptide Sequences in LOV Proteins Modulates Bcl‐2 Family Interactions
Author(s) -
Mart Robert J.,
Meah Dilruba,
Allemann Rudolf. K.
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500469
Subject(s) - phototropin , flavin group , covalent bond , chemistry , cryptochrome , biophysics , peptide , optogenetics , amphiphile , apoptosis , microbiology and biotechnology , biochemistry , biology , enzyme , circadian clock , organic chemistry , neuroscience , copolymer , gene , polymer
LOV domains act as biomolecular sensors for light, oxygen or the environment's redox potential. Conformational changes upon the formation of a covalent cysteinyl flavin adduct are propagated through hydrogen‐bonding networks in the core of designed hybrid phototropin LOV2 domains that incorporate the Bcl homology region 3 (BH3) of the key pro‐apoptotic protein BH3‐interacting‐domain death agonist (BID). The resulting change in conformation of a flanking amphiphilic α‐helix creates a light‐dependent optogenetic tool for the modulation of interactions with the anti‐apoptotic B‐cell leukaemia‐2 (Bcl‐2) family member Bcl‐x L .
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