Sandbox Reserved 1712: Difference between revisions

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Once the ALKAL binds with ALK and dimerizes with another ALK-ALKAL complex, this activated conformation also initiates a conformational change of the intracellular kinase domain of ALK. This causes an autophosphorylation of several tyrosine residues of this domain, activating a signaling cascade with its kinase activity.

== Disease ==

There are many <scene name='90/~~904318~~/Premutationresidues/2'>residues that could be mutated</scene> that would cause constitutive receptor activation, enhancement between the interaction of receptors or stabilization of active receptors are known to relate to oncogenic potentials (Figure 4). The <scene name='90/~~904318~~/His694/2'>His694</scene> that is mutated to an arginine is known to be a gain-of-function in lung adenocarcinoma which can lead to constitutive activation of ALK. The <scene name='90/~~904318~~/Phe856/1'>Phe856</scene> that is mutated to the a serine may cause a gain-of-function mutation that is linked to acute myeloid leukemia. When the <scene name='90/904318/Arg753/2'>Arg753</scene> is mutated to a glutamate it is commonly identified in histiocytic neoplasms. The <scene name='90/904318/Gly747/1'>Gly747</scene> changing to arginine could cause possible oncogenic potentials which are not specified yet. The F856S and R753Q mutations are known to increase cytokine-dependent cell proliferation in certain cells. <ref>DOI:10.1038/s41586-021-03959-5</ref>

There are many <scene name='90/904317/Premutationresidues/1'>residues that could be mutated</scene> that would cause constitutive receptor activation, enhancement between the interaction of receptors or stabilization of active receptors are known to relate to oncogenic potentials (Figure 4). The <scene name='90/904317/His694/1'>His694</scene> that is mutated to an arginine is known to be a gain-of-function in lung adenocarcinoma which can lead to constitutive activation of ALK. The <scene name='90/904317/Phe856/1'>Phe856</scene> that is mutated to the a serine may cause a gain-of-function mutation that is linked to acute myeloid leukemia. When the <scene name='90/904318/Arg753/2'>Arg753</scene> is mutated to a glutamate it is commonly identified in histiocytic neoplasms. The <scene name='90/904318/Gly747/1'>Gly747</scene> changing to arginine could cause possible oncogenic potentials which are not specified yet. The F856S and R753Q mutations are known to increase cytokine-dependent cell proliferation in certain cells. <ref>DOI:10.1038/s41586-021-03959-5</ref>

[[Image:Mutations.png|800 px|left|thumb|Figure 4: Mutated residues on ALK that contribute to stabilization of the active state of ALK, leading to many types of cancers. From left to right: F856S, G747R, H694R, R753Q]]

</StructureSection>

== References ==

Sandbox Reserved 1712: Difference between revisions

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@@ Line 19: / Line 19: @@
 Once the ALKAL binds with ALK and dimerizes with another ALK-ALKAL complex, this activated conformation also initiates a conformational change of the intracellular kinase domain of ALK. This causes an autophosphorylation of several tyrosine residues of this domain, activating a signaling cascade with its kinase activity.
 == Disease ==
-There are many <scene name='90/904318/Premutationresidues/2'>residues that could be mutated</scene> that would cause constitutive receptor activation, enhancement between the interaction of receptors or stabilization of active receptors are known to relate to oncogenic potentials (Figure 4). The <scene name='90/904318/His694/2'>His694</scene> that is mutated to an arginine is known to be a gain-of-function in lung adenocarcinoma which can lead to constitutive activation of ALK. The <scene name='90/904318/Phe856/1'>Phe856</scene> that is mutated to the a serine may cause a gain-of-function mutation that is linked to acute myeloid leukemia. When the <scene name='90/904318/Arg753/2'>Arg753</scene> is mutated to a glutamate it is commonly identified in histiocytic neoplasms. The <scene name='90/904318/Gly747/1'>Gly747</scene> changing to arginine could cause possible oncogenic potentials which are not specified yet. The F856S and R753Q mutations are known to increase cytokine-dependent cell proliferation in certain cells. <ref>DOI:10.1038/s41586-021-03959-5</ref>
+There are many <scene name='90/904317/Premutationresidues/1'>residues that could be mutated</scene> that would cause constitutive receptor activation, enhancement between the interaction of receptors or stabilization of active receptors are known to relate to oncogenic potentials (Figure 4). The <scene name='90/904317/His694/1'>His694</scene> that is mutated to an arginine is known to be a gain-of-function in lung adenocarcinoma which can lead to constitutive activation of ALK. The <scene name='90/904317/Phe856/1'>Phe856</scene> that is mutated to the a serine may cause a gain-of-function mutation that is linked to acute myeloid leukemia. When the <scene name='90/904318/Arg753/2'>Arg753</scene> is mutated to a glutamate it is commonly identified in histiocytic neoplasms. The <scene name='90/904318/Gly747/1'>Gly747</scene> changing to arginine could cause possible oncogenic potentials which are not specified yet. The F856S and R753Q mutations are known to increase cytokine-dependent cell proliferation in certain cells. <ref>DOI:10.1038/s41586-021-03959-5</ref>
 [[Image:Mutations.png|800 px|left|thumb|Figure 4: Mutated residues on ALK that contribute to stabilization of the active state of ALK, leading to many types of cancers. From left to right: F856S, G747R, H694R, R753Q]]
 </StructureSection>
 == References ==
 <references/>