Sandbox122: Difference between revisions

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Blue light arrives on the only LOV2 <scene name='Sandbox122/Cystein_residue/1'>cystein residue</scene>(situate 4.2A from atom C(4a)) and induces formation of covalent cysteinyl-C(4a)adduct. (To explain that, refer to the scheme). Somes studies showed that temperature have an influence on that adduct. In fact, at low temperature, the microenvironment determine the reactivity of the S-H group of Cys966. A base-catalyzed mechanism for dark state recovery. Imidazole snatch proton from N5 atom of FMN and give it to the cysteine again (explain on the scheme).
Blue light arrives on the only LOV2 <scene name='Sandbox122/Cystein_residue/1'>cystein residue</scene>(situate 4.2A from atom C(4a)) and induces formation of covalent cysteinyl-C(4a)adduct. (To explain that, refer to the scheme). Somes studies showed that temperature have an influence on that adduct. In fact, at low temperature, the microenvironment determine the reactivity of the S-H group of Cys966. A base-catalyzed mechanism for dark state recovery. Imidazole snatch proton from N5 atom of FMN and give it to the cysteine again (explain on the scheme).
==LOV2 signal transmission==
==LOV2 signal transmission==
studies have implicated a role for the central β-sheet scaffold in propagating the signal generated within the FMN-binding pocket to protein changes at the LOV2 surface, which are necessary for activation of the C-terminal kinase domain.21,22 Specifically, the side chain of a conserved glutamine residue within LOV2 (Gln575 in Arabidopsis phot1) which forms hydrogen bonds with the FMN chromophore flips by 180° upon cysteinyl adduct formation11,23,24 causing protein changes in the central β-sheet scaffold that forms contacts with the Jα-helix.
Some studies have showed a role for the central β-sheet in propagating the signal generated within the FMN-protein changes at the LOV2 surface, which are necessary for activation of the C-terminal kinase domain.Specifically, the side chain of a conserved glutamine residue within LOV2 (Gln575 in Arabidopsis phot1) which forms hydrogen bonds with the FMN chromophore flips by 180° upon cysteinyl adduct formation causing protein changes in the central β-sheet that forms contacts with the Jα-helix.
  This complex may interact directly with the kinase and regulate his activity.  
  This complex may interact directly with the kinase and regulate his activity.  
==Kinase regulation by LOV2==
==Kinase regulation by LOV2==