Photocontrolled Exposure of Pro-apoptotic Peptide Sequences in LOV Proteins Modulates Bcl-2 Family Interactions.
Photocontrolled Exposure of Pro-apoptotic Peptide Sequences in LOV Proteins Modulates Bcl-2 Family Interactions.
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DOI:
10.1002/cbic.201500469
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发表时间:
2016-04-15
期刊:
影响因子:
3.2
通讯作者:
Allemann, Rudolf. K.
中科院分区:
文献类型:
--
作者:
Mart, Robert J.;Meah, Dilruba;Allemann, Rudolf. K.
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‐xL.
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