User:Sean Callahan/Sandbox 1: Difference between revisions

LSD-1 is a protein that can be regulated by outside factors. The tower domain and oxidase domain are connected by a <scene name='81/811711/Regulator_loop/6'>tower oxidase connector</scene>. 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<ref name="Stavropoulos">PMID: 16799558</ref>.

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 [http://proteopedia.org/wiki/index.php/Androgen_receptor#Function 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<ref name="Stavropoulos">PMID: 16799558</ref>.