Sandbox Reserved 1713

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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.

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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 Anaplastic Lymphoma Kinase is a receptor tyrosine kinase. ALK transfers a phosphate group from ATP to a tyrosine residue on an enzyme which activates a signaling cascade, and ALK becomes activated when a ligand called ALKAL binds to the binding surface on an extracellular domain of ALK. ALK is an integral membrane protein. Function Figure 1 Figure 2 interacting residues of ALK and ALKAL ALK-ALKAL binding surface structure of the glycine-rich domain Binding surface of ALKAL with the membrane ALKAL's residues that interact with membrane Conformational Change In order for the Anaplastic Lymphoma Kinase (ALK) to move across the membrane to bind with the second monomer, it has to undergo a conformational change. The Anaplastic Lymphoma Kinase Activating Ligand (ALKAL) binds to the binding surface on the ALK. This induces a conformational change which allows for the PXL and the GlyR domains to hinge forward. The kinase is now ready to move across the membrane and attach to the other kinase to be fully activated. Movement across the membrane The negatively charged phosphate groups on the cell membrane interact with the highly conserved positively charged residues on ALKAL ligand that face the membrane, which stabilizes the ligand to bind to ALK even better. Disease mutated residues His694 Phe856 Arg753 Structural highlights The active state of the kinase is when two monomers have completed a conformational change and moved across the membrane to form a dimer.