Sandbox Reserved 1726

This Sandbox is Reserved from February 28 through September 1, 2022 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1700 through Sandbox Reserved 1729.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. 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

Anaplastic Lymphoma Kinase

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. Structure Domains Three Helix Bundle-like Domain The three helix bundle-like domain mainly has a structural function overall as it interacts with the tumor necrosis factor-like domain upon ligand binding. Poly-Glycine Domain Located between the three helix bundle-like domain and the tumor necrosis factor-like domain, the poly-glycine domain has an important structural role. Tumor Necrosis Factor-like Domain The tumor necrosis factor-like domain interacts with the three helix bundle-like domain to begin the conformational changes associated with ligand binding. The three helix bundle-like domain's α-helix interacts with the helix α-1' and β strand A-1'. This domain also assists in mediating ligand binding with the epidermal growth factor-like domain. Epidermal Growth Factor-like Domain The epidermal growth factor-like domain is very malleable and repositioning of this domain is essential for activation of the protein. This domain is able to undergo conformational changes with the ligand bound and when in contact with the tumor necrosis factor-like domain. Binding Site The binding site of Anaplastic Lymphoma Kinase is approximately from E859 to D1006 on one monomer. This site doesn't start out surrounding the ligand, instead the proximity of the ligand allows conformational changes across the protein. Dimerization of Anaplastic Lymphoma Kinase To achieve 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.