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Introduction
SWIRM Domain
Disease
Reddit
Regulation
Allosteric Stie
LSD-1 can be regulated by outside factors. The tower domain and oxidase domain are connected by a . The oxidase domain is what harbors the catalytic chamber for LSD-1. Any change to the catalytic chamber could drastically reduce the ability for the methylated lysine of the substrate to fit in the binding site correctly. Because the tower domain is attached to the oxidase domain, the tower domain and the connector region may allosterically regulate demethylase activity. Any interaction with these two sites is hypothesized to change the enzyme activity. This has further pushed the assumption that the CoRest complex effects enzyme activity via interaction with the tower domain.[3]
Androgen Receptor
LSD-1 will demethylate mono or di-methylated lysines. It will only demethylate lysine 4 of histone 3. This factor can be regulated by the androgen receptor which can change its specificity for a different target.[4] The androgen receptor is a steroid hormone receptor that can modulate 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.[5]
Relevance
Structural highlights
Hey will show the FAD
And will show you the oxidase domain
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