Sandbox Reserved 1705: Difference between revisions

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=== Ligand Binding===

The ligands utilized by anaplastic lymphoma kinase are monomeric FAM150 and <scene name='90/904310/Ligand/1'>dimeric AUG</scene>. It's biologically preferred ligand is dimeric AUG. The binding of ALK to it's ligand causes results in homodimerization and a conformational change. Prior to the ligand binding to anaplastic lymphoma kinase, the extracellular domain is oriented sticking up perpendicularly to the plasma membrane. Once the ligand is <scene name='90/904310/Dimer_ligand_complex/3'>bound</scene>, ALK undergoes a conformational change and folds over so that the positively charged residues on the portion of the protein previously sticking up perpendicularly is now interacting to the negatively charged residues on the plasma membrane. Once the ligand is bound and the conformational change has occurred, the kinase domain is auto-activated in which the domains use the tyrosine phosphorylation mechanism to phosphorylate the tyrosine residue on the opposite monomer.

The ligands utilized by anaplastic lymphoma kinase are monomeric FAM150 and <scene name='90/904310/Ligand/1'>dimeric AUG</scene>. It's biologically preferred ligand is dimeric AUG. The binding of ALK to it's ligand causes results in homodimerization and a conformational change. Prior to the ligand binding to anaplastic lymphoma kinase, the extracellular domain is oriented sticking up perpendicularly to the plasma membrane. Once the ligand is <scene name='90/904310/Dimer_ligand_complex/3'>bound</scene>, ALK undergoes a conformational change and folds over so that the positively charged residues on the portion of the protein previously sticking up perpendicularly is now interacting to the negatively charged residues on the plasma membrane. These residues interact through the formation of <scene name='90/904310/Dimer-ligand-interface/4'>salt bridges</scene>. Once the ligand is bound and the conformational change has occurred, the kinase domain is auto-activated in which the domains use the tyrosine phosphorylation mechanism to phosphorylate the tyrosine residue on the opposite monomer.

==== Tyrosine Phosphorylation Mechanism ====

Sandbox Reserved 1705: Difference between revisions

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@@ Line 11: / Line 11: @@
 === Ligand Binding===
-The ligands utilized by anaplastic lymphoma kinase are monomeric FAM150 and <scene name='90/904310/Ligand/1'>dimeric AUG</scene>. It's biologically preferred ligand is dimeric AUG. The binding of ALK to it's ligand causes results in homodimerization and a conformational change. Prior to the ligand binding to anaplastic lymphoma kinase, the extracellular domain is oriented sticking up perpendicularly to the plasma membrane. Once the ligand is <scene name='90/904310/Dimer_ligand_complex/3'>bound</scene>, ALK undergoes a conformational change and folds over so that the positively charged residues on the portion of the protein previously sticking up perpendicularly is now interacting to the negatively charged residues on the plasma membrane. Once the ligand is bound and the conformational change has occurred, the kinase domain is auto-activated in which the domains use the tyrosine phosphorylation mechanism to phosphorylate the tyrosine residue on the opposite monomer.
+The ligands utilized by anaplastic lymphoma kinase are monomeric FAM150 and <scene name='90/904310/Ligand/1'>dimeric AUG</scene>. It's biologically preferred ligand is dimeric AUG. The binding of ALK to it's ligand causes results in homodimerization and a conformational change. Prior to the ligand binding to anaplastic lymphoma kinase, the extracellular domain is oriented sticking up perpendicularly to the plasma membrane. Once the ligand is <scene name='90/904310/Dimer_ligand_complex/3'>bound</scene>, ALK undergoes a conformational change and folds over so that the positively charged residues on the portion of the protein previously sticking up perpendicularly is now interacting to the negatively charged residues on the plasma membrane. These residues interact through the formation of <scene name='90/904310/Dimer-ligand-interface/4'>salt bridges</scene>. Once the ligand is bound and the conformational change has occurred, the kinase domain is auto-activated in which the domains use the tyrosine phosphorylation mechanism to phosphorylate the tyrosine residue on the opposite monomer.
 ==== Tyrosine Phosphorylation Mechanism ====