Understanding JMJD2A's Selectivity for Methylation States
Author Information
Author(s): Ulucan Ozlem, Keskin Ozlem, Erman Burak Gursoy, Attila
Primary Institution: Center for Computational Biology and Bioinformatics and College of Engineering, Koc University, Istanbul, Turkey
Hypothesis
How does JMJD2A discriminate between different methylation states of histone tails?
Conclusion
The study reveals that JMJD2A's selectivity for methylation states is influenced by the orientation and proximity of methyl groups to the Fe(II) ion.
Supporting Evidence
- JMJD2A selectively demethylates specific lysine residues on histone tails.
- Binding free energy calculations indicate that JMJD2A has the highest affinity for trimethylated lysine.
- Hydrogen bonding analysis shows that interactions between JMJD2A and its substrates are primarily main chain-side chain interactions.
Takeaway
JMJD2A is like a key that only fits certain locks, and it can tell the difference between similar locks based on how they are shaped and where they are located.
Methodology
The study used molecular dynamics simulations to analyze the interactions between JMJD2A and methylated histone tails.
Limitations
The study is based on computational simulations, which may not fully capture the complexity of biological systems.
Digital Object Identifier (DOI)
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