Sandbox Reserved 1656

This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Deubiquitinase

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. 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 or to the article describing Jmol to the rescue. Generalities Function Deubiquitinases or Deubiquitinating enzymes (DUBs) are key enzymes belonging to the vast group of proteases, allowing the degradation of ubiquitin of proteins. These enzymes are thus implicated in the regulation of protein degradation. Indeed, when a protein is going to be degraded, an enzymatic cascade will add a poly-ubiquitin fragment to the protein. This mechanism is called ubiquitination.[1] Following this step, mono or poly-ubiquitin is removed from the protein which has been degraded, by deubiquitinase. Families Deubiquitinases belong to the protease family. This family is divided into five classes, according to the nature of the amino acid composition of their active site carrying out the catalysis: serine protease, cysteine proteases, acid proteases, metalloproteases, threonine proteases. DUBs belong to only two of these families: metalloproteases and cysteine proteases. Among the cysteine proteins, four subfamilies can be described according to their catalytic domains: ubiquitin-specific proteases (USP), les Ubiquitin C-terminal hydrolases (UCH), les Otubain proteases (OTU) et les Machado-joseph disease proteases (MJD). The deubiquitinases belonging to the family of metalloproteases all have a JAMM catalytic domain (JAB1/MPN/Mov34 metalloenzyme). Disease The involvement of deubiquitinases in diseases is still poorly understood. However, it is known that they play a role in various physiological processes, particularly in the case of cancers. Structural highlights This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.