Sandbox Reserved 1704: Difference between revisions
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== General Structure == | == General Structure == | ||
Anaplastic lymphoma kinase is a homodimer, each monomer consisting of seven domains and two regions. These domains and regions are as follows: N-terminal region (NTR), two meprin–A-5 protein–receptor protein tyrosine phosphatase μ domains (MAM), low density lipoprotein receptor class A domain (LDL), tumor necrosis factor receptor-like domain (TNF), glycine rich region (GlyR), epidermal growth factor receptor-like domain (EGF), transmembrane α-helix (TMH), kinase domain <ref name="Reshetnyak">PMID:34819673</ref>. The structures of the N-terminal region, MAM, and LDL have not been determined. The glycine rich region is a part of the TNF domain. Only the TNF, GlyR, and EGF portions of ALK are required for ligand binding. All portions of anaplastic lymphoma kinase are located in the extracellular domain except for the transmembrane α-helix which is in the transmembrane region and the kinase domain that is located in the intracellular domain. | Anaplastic lymphoma kinase is a homodimer, each monomer consisting of seven domains and two regions. These domains and regions are as follows: N-terminal region (NTR), two meprin–A-5 protein–receptor protein tyrosine phosphatase μ domains (MAM), low density lipoprotein receptor class A domain (LDL), tumor necrosis factor receptor-like domain (TNF), glycine rich region (GlyR), epidermal growth factor receptor-like domain (EGF), transmembrane α-helix (TMH), kinase domain <ref name="Reshetnyak">PMID:34819673</ref>. The structures of the N-terminal region, MAM, and LDL have not been determined. The glycine rich region is a part of the TNF domain. Only the TNF, GlyR, and EGF portions of ALK are required for ligand binding. All portions of anaplastic lymphoma kinase are located in the extracellular domain except for the transmembrane α-helix which is in the transmembrane region and the kinase domain that is located in the intracellular domain. [[Image:ALK_Domain_Outline.png|350 px|right|thumb|Figure 1. Outline of the domains and regions of anaplastic lymphoma kinase]] | ||
=== Ligand Binding=== | === Ligand Binding=== | ||
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==== Tyrosine Phosphorylation Mechanism ==== | ==== Tyrosine Phosphorylation Mechanism ==== | ||
Dimerization of anaplastic lymphoma kinase activates the kinase domains of each monomer. Next, the kinase domains phosphorylate the tyrosine residues of the opposite monomer using ATP. These phosphorylated tyrosine residues recruit signal proteins through phosphorylation. These signal proteins begin a signaling cascade through utilizing various signal pathways. These pathways signal for cell proliferation and survival (ex: begin transcription). | Dimerization of anaplastic lymphoma kinase activates the kinase domains of each monomer. Next, the kinase domains phosphorylate the tyrosine residues of the opposite monomer using ATP. These phosphorylated tyrosine residues recruit signal proteins through phosphorylation. These signal proteins begin a signaling cascade through utilizing various signal pathways. These pathways signal for cell proliferation and survival (ex: begin transcription). [[Image:Tyrosine_Mechanism_Picture.png|350 px|right|thumb|Figure 1. Tyrosine phosphorylation mechanism]] | ||
== Applications == | == Applications == | ||
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== References == | == References == | ||
<references/> | <references/> | ||
== Student Contributors == | |||
*Kaylin Todor | |||
*Rebekah White | |||
