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Introduction
SWIRM Domain
Disease
Reddit
Headline
Allosteric Stie
LSD-1 is a protein that can be regulated by outside factors. The tower domain and oxidase domain are connected by a . The oxidase domain is what holds the catalytic chamber for LSD-1. This makes the oxidase domain a very sensitive domain. Any change to the catalytic chamber could drastically reduce the ability for the methylated amine to fit in the binding site correctly. Because the tower domain is attached to the oxidase domain, the tower domain and the connector region become allosteric sites. Any interaction with these two sites is hypothesized to drastically change the enzyme activity. This has further pushed the assumption that the CoRest complex interacts with the tower region.
Androgen Receptor
LSD-1 will demethylate mono or di-methylated lysines. However it will not demethylate just any lysine. It will only demethylate lysine H3-K4. This factor can be regulated by the androgen receptor. The androgen receptor is a protein that is involved in DNA transcription. When it interacts with LSD-1 it will no longer demethylate H3-K4, but will now demethylate H3-K9. This attribute allows LSD-1 to work on a wider range of residues.
Relevance
Structural highlights
Hey will show the FAD
And will show you the oxidase domain
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