User:Sean Callahan/Sandbox 1: Difference between revisions

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The interactions between the SWIRM and Oxidase domains create a <scene name='81/811711/Swirm-oxidase_interface/1'>cleft</scene> through a number of hydrophobic (van der Waals) interactions. The interior ends of the helices in the SWIRM domain contribute to the cleft, as well as the alpha helices from the oxidase domains. Because of its vicinity to the active site and FAD co-factor, it is believed that this cleft may serve as a site for additional histone tail binding<ref name="Stavropoulos">PMID: 16799558</ref>.
The interactions between the SWIRM and Oxidase domains create a <scene name='81/811711/Swirm-oxidase_interface/1'>cleft</scene> through a number of hydrophobic (van der Waals) interactions. The interior ends of the helices in the SWIRM domain contribute to the cleft, as well as the alpha helices from the oxidase domains. Because of its vicinity to the active site and FAD co-factor, it is believed that this cleft may serve as a site for additional histone tail binding<ref name="Stavropoulos">PMID: 16799558</ref>.
===Tower Domain===
===Tower Domain===
A unique and defining feature of LSD1 is the 100 residue long insertion between the two parts of the oxidase domain in the primary structure. This <scene name='81/811711/Tower_domain/1'>Tower Domain</scene> spans from residues 419-520. This domain is unique, yet vital to LSD1 function. Specifically, it is hypothesized to be a binding platform of LSD1 to the CoRest complex, as well as a site of allosteric regulation. The CoRest complex is a group of proteins responsible for the silencing of neuronal genes in non-neural cells, and the binding of LSD1 to this complex activates its demethylase activity. It is composed to two long alpha helices(TaA and TaB) that extend from the core of the protein. The helices hold each other in place through hydrophobic interactions. The TaB helix is the shorter of the two and is connected to a helix in the oxidase domain (aD). aD is essential for active site formation, and TaB is thought to be responsible for the correct <scene name='81/811711/Tab_and_ad_helix_interaction/1'>positioning</scene> of aD<ref name="Stavropoulos">PMID: 16799558</ref>.
A unique and defining feature of LSD1 is the 100 residue long insertion between the two parts of the oxidase domain in the primary structure. This <scene name='81/811711/Tower_domain/1'>Tower Domain</scene> spans from residues 419-520. This domain is unique, yet vital to LSD1 function. Specifically, it is hypothesized to be a binding platform of LSD1 to the [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3048046/ CoREST complex] , as well as a site of allosteric regulation. The CoREST complex is a group of proteins responsible for the silencing of neuronal genes in non-neural cells, and the binding of LSD1 to this complex activates its demethylase activity. It is composed to two long alpha helices(TaA and TaB) that extend from the core of the protein. The helices hold each other in place through hydrophobic interactions. The TaB helix is the shorter of the two and is connected to a helix in the oxidase domain (aD). aD is essential for active site formation, and TaB is thought to be responsible for the correct <scene name='81/811711/Tab_and_ad_helix_interaction/1'>positioning</scene> of aD<ref name="Stavropoulos">PMID: 16799558</ref>.


==Regulation==
==Regulation==
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