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Photocontrolled exposure of pro-apoptotic peptide sequences in LOV proteins modulate Bcl-2 family interactions

Mart, Robert, Meah, Dilruba and Allemann, Rudolf Konrad 2016. Photocontrolled exposure of pro-apoptotic peptide sequences in LOV proteins modulate Bcl-2 family interactions. Chembiochem 17 (8) , pp. 698-701. 10.1002/cbic.201500469

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Abstract

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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Subjects: Q Science > QD Chemistry
Publisher: Wiley-Blackwell
ISSN: 1439-4227
Funders: Biotechnology and Biological Sciences Research Council
Date of First Compliant Deposit: 30 March 2016
Date of Acceptance: 22 October 2015
Last Modified: 04 Jun 2017 08:45
URI: http://orca.cf.ac.uk/id/eprint/84159

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