Front Cover: Targeting Zinc Finger Proteins with Exogenous Metals and Molecules: Lessons Learned from Tristetraprolin, a CCCH type Zinc Finger (Eur. J. Inorg. Chem. 37/2021)
Kiwon Ok, Miloš R. Filipović, Sarah L. J. Michel
Abstract
Kiwon Ok, Miloš R. Filipović, Sarah L. J. Michel
Abstract
The Front Cover shows the many ways that the zinc finger protein tristetraprolin (TTP) can be targeted by exogenous metals (e.g. Cd, Au) and endogenous signaling molecules (e.g. H2S). TTP has limited secondary structure and the cysteine residues that coordinate the native zinc co-factor are exposed for reactivity with exogenous and endogenous molecules. TTP binds with high sequence specificity to the mRNA sequence AAAUAAAUAAA from inflammatory cytokines. When TTP is bound to its mRNA target, metal or signaling molecule exchange can be abrogated due to a protective effect of the mRNA. More information can be found in the Minireview by S. L. J. Michel and co-workers.
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The Front Cover shows the many ways that the zinc finger protein tristetraprolin (TTP) can be targeted by exogenous metals (e.g. Cd, Au) and endogenous signaling molecules (e.g. H2S). TTP has limited secondary structure and the cysteine residues that coordinate the native zinc co-factor are exposed for reactivity with exogenous and endogenous molecules. TTP binds with high sequence specificity to the mRNA sequence AAAUAAAUAAA from inflammatory cytokines. When TTP is bound to its mRNA target, metal or signaling molecule exchange can be abrogated due to a protective effect of the mRNA. More information can be found in the Minireview by S. L. J. Michel and co-workers.
Key concepts: Tristetraprolin, Zinc finger, Chemistry, Zinc, Cysteine, Endogeny, Molecule, Front cover