Sandbox Reserved 1726: Difference between revisions
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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 alpha helix interacts with the helix alpha-1' and beta strand A-1'. This domain also assists in mediating ligand binding with the epidermal growth 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 alpha helix interacts with the helix alpha-1' and beta strand A-1'. This domain also assists in mediating ligand binding with the epidermal growth factor-like domain. | ||
==== 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. | 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 | |||
== Function == | == Function == | ||
