User:Andrew Hesterhagen/Sandbox 1

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

This is a default text for your page Andrew Hesterhagen/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Introduction

SWIRM Domain

Figure 1

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

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.