Sandbox Reserved 1705: Difference between revisions

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== General Structure ==

Anaplastic lymphoma kinase is a <scene name='90/904310/Dimer/2'>homodimer</scene>, each monomer consisting of seven domains and two regions <ref name="Tongqing">PMID:34819665</ref>. 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), <scene name='90/904310/Tnf_highlighted_monomer/2'>tumor necrosis factor receptor-like domain</scene> (TNF), <scene name='90/904310/Glyr_highlighted_monomer/1'>glycine rich region</scene>(GlyR), <scene name='90/904310/Egf_highlighted_monomer/1'>epidermal growth factor receptor-like domain</scene> (EGF), transmembrane α-helix (TMH), kinase domain <ref name="Reshetnyak">PMID:34819673</ref>. The NTR functions as a signal peptide, the structure of which is yet to be determined. Though the biological roles and structures of MAM and LDL have not been determined, they are a very unique component to ALK. ALK is the only RTK that has two MAM domains and a LDL domain. Studies of other MAM domains have suggested that MAM may play a role in cell-cell interactions through homophilic binding <ref name="Huang">PMID: 30400214</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 region.

Anaplastic lymphoma kinase is a <scene name='90/904310/Dimer/2'>homodimer</scene>, each monomer consisting of seven domains and two regions <ref name="Tongqing">PMID:34819665</ref>. 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), <scene name='90/904310/Tnf_highlighted_monomer/2'>tumor necrosis factor receptor-like domain</scene> (TNF), <scene name='90/904310/Glyr_highlighted_monomer/1'>glycine rich region</scene>(GlyR), <scene name='90/904310/Egf_highlighted_monomer/1'>epidermal growth factor receptor-like domain</scene> (EGF), transmembrane α-helix (TMH), kinase domain <ref name="Reshetnyak">PMID:34819673</ref>. The NTR functions as a signal peptide, the structure of which is yet to be determined. Though the biological roles and structures of MAM and LDL have not been determined, they are a very unique component to ALK. ALK is the only RTK that has two MAM domains and a LDL domain. Studies of other MAM domains have suggested that MAM may play a role in cell-cell interactions through homophilic binding <ref name="Huang">PMID: 30400214</ref>. The TNF-like domain assists in mediating mature T-cell receptor induced apoptosis. The glycine rich region is a part of the TNF domain. The GlyR region consists of multiple glycine helices which is a highly unique structure. Though the function of ALK's EGF domain is unknown, we do know that all EGF domains are found in the extracellular region and are thought to be important building blocks for extracellular proteins <ref name="Selander-Sunnerhagen">PMID:1527084</ref>. The structures of the N-terminal region, MAM, and LDL have not been determined. 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 region.

=== Ligand Binding===

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 == General Structure ==
-Anaplastic lymphoma kinase is a <scene name='90/904310/Dimer/2'>homodimer</scene>, each monomer consisting of seven domains and two regions <ref name="Tongqing">PMID:34819665</ref>. 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), <scene name='90/904310/Tnf_highlighted_monomer/2'>tumor necrosis factor receptor-like domain</scene> (TNF), <scene name='90/904310/Glyr_highlighted_monomer/1'>glycine rich region</scene>(GlyR), <scene name='90/904310/Egf_highlighted_monomer/1'>epidermal growth factor receptor-like domain</scene> (EGF), transmembrane α-helix (TMH), kinase domain <ref name="Reshetnyak">PMID:34819673</ref>. The NTR functions as a signal peptide, the structure of which is yet to be determined. Though the biological roles and structures of MAM and LDL have not been determined, they are a very unique component to ALK. ALK is the only RTK that has two MAM domains and a LDL domain. Studies of other MAM domains have suggested that MAM may play a role in cell-cell interactions through homophilic binding <ref name="Huang">PMID: 30400214</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 region.
+Anaplastic lymphoma kinase is a <scene name='90/904310/Dimer/2'>homodimer</scene>, each monomer consisting of seven domains and two regions <ref name="Tongqing">PMID:34819665</ref>. 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), <scene name='90/904310/Tnf_highlighted_monomer/2'>tumor necrosis factor receptor-like domain</scene> (TNF), <scene name='90/904310/Glyr_highlighted_monomer/1'>glycine rich region</scene>(GlyR), <scene name='90/904310/Egf_highlighted_monomer/1'>epidermal growth factor receptor-like domain</scene> (EGF), transmembrane α-helix (TMH), kinase domain <ref name="Reshetnyak">PMID:34819673</ref>. The NTR functions as a signal peptide, the structure of which is yet to be determined. Though the biological roles and structures of MAM and LDL have not been determined, they are a very unique component to ALK. ALK is the only RTK that has two MAM domains and a LDL domain. Studies of other MAM domains have suggested that MAM may play a role in cell-cell interactions through homophilic binding <ref name="Huang">PMID: 30400214</ref>. The TNF-like domain assists in mediating mature T-cell receptor induced apoptosis. The glycine rich region is a part of the TNF domain. The GlyR region consists of multiple glycine helices which is a highly unique structure. Though the function of ALK's EGF domain is unknown, we do know that all EGF domains are found in the extracellular region and are thought to be important building blocks for extracellular proteins <ref name="Selander-Sunnerhagen">PMID:1527084</ref>. The structures of the N-terminal region, MAM, and LDL have not been determined.  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 region.
 === Ligand Binding===