Sandbox Reserved 1627: Difference between revisions

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===Conformation Change===

When the receptor is in an <scene name='83/832953/Inactive_insulin_receptor/4'>inverted V</scene> shape, the FnIII-3 domains are separated by about 120Å. <ref name= "Mckern"> PMID: 16957736</ref> This distance prevents the initiation of autophosphorylation and downstream signaling by the tyrosine kinase domains on the intracellular side of the receptor. Upon the binding of insulin to three binding sites, 1, 1', and either 2 or 2', the conformation change will begin and bring the FnIII-3 domains within 40Å of each other to induce the <scene name='83/832953/Ir_dimer_t_state/3'>T shape</scene> conformation. <ref> DOI 10.1038/s41467-018-06826-6</ref> <ref name="Uchikawa" /> The T shape conformation is well observed in the alpha subunit. It is horizontally composed of L1, CR (including the <scene name='83/832953/Alpha_c_helix/9'>α-CT chain</scene>), and L2 domains and vertically composed of the FnIII-1, 2, and 3 domains (Figure 1). The insulin receptor's structural [http://en.wikipedia.org/wiki/Conformational_change conformation change] is what allows it to go from the inactive state to the active state in order to facilitate the autophosphorylation of the tyrosine kinase domain.

When the receptor is in an <scene name='83/832953/Inactive_insulin_receptor/5'>inverted V</scene> shape, the FnIII-3 domains are separated by about 120Å. <ref name= "Mckern"> PMID: 16957736</ref> This distance prevents the initiation of autophosphorylation and downstream signaling by the tyrosine kinase domains on the intracellular side of the receptor. Upon the binding of insulin to three binding sites, 1, 1', and either 2 or 2', the conformation change will begin and bring the FnIII-3 domains within 40Å of each other to induce the <scene name='83/832953/Ir_dimer_t_state/3'>T shape</scene> conformation. <ref> DOI 10.1038/s41467-018-06826-6</ref> <ref name="Uchikawa" /> The T shape conformation is well observed in the alpha subunit. It is horizontally composed of L1, CR (including the <scene name='83/832953/Alpha_c_helix/9'>α-CT chain</scene>), and L2 domains and vertically composed of the FnIII-1, 2, and 3 domains (Figure 1). The insulin receptor's structural [http://en.wikipedia.org/wiki/Conformational_change conformation change] is what allows it to go from the inactive state to the active state in order to facilitate the autophosphorylation of the tyrosine kinase domain.

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 ===Conformation Change===
-When the receptor is in an <scene name='83/832953/Inactive_insulin_receptor/4'>inverted V</scene> shape, the FnIII-3 domains are separated by about 120Å. <ref name= "Mckern"> PMID: 16957736</ref> This distance prevents the initiation of autophosphorylation and downstream signaling by the tyrosine kinase domains on the intracellular side of the receptor. Upon the binding of insulin to three binding sites, 1, 1', and either 2 or 2', the conformation change will begin and bring the FnIII-3 domains within 40Å of each other to induce the <scene name='83/832953/Ir_dimer_t_state/3'>T shape</scene> conformation. <ref> DOI 10.1038/s41467-018-06826-6</ref> <ref name="Uchikawa" /> The T shape conformation is well observed in the alpha subunit. It is horizontally composed of L1, CR (including the <scene name='83/832953/Alpha_c_helix/9'>α-CT chain</scene>), and L2 domains and vertically composed of the FnIII-1, 2, and 3 domains (Figure 1). The insulin receptor's  structural [http://en.wikipedia.org/wiki/Conformational_change conformation change] is what allows it to go from the inactive state to the active state in order to facilitate the autophosphorylation of the tyrosine kinase domain.
+When the receptor is in an <scene name='83/832953/Inactive_insulin_receptor/5'>inverted V</scene> shape, the FnIII-3 domains are separated by about 120Å. <ref name= "Mckern"> PMID: 16957736</ref> This distance prevents the initiation of autophosphorylation and downstream signaling by the tyrosine kinase domains on the intracellular side of the receptor. Upon the binding of insulin to three binding sites, 1, 1', and either 2 or 2', the conformation change will begin and bring the FnIII-3 domains within 40Å of each other to induce the <scene name='83/832953/Ir_dimer_t_state/3'>T shape</scene> conformation. <ref> DOI 10.1038/s41467-018-06826-6</ref> <ref name="Uchikawa" /> The T shape conformation is well observed in the alpha subunit. It is horizontally composed of L1, CR (including the <scene name='83/832953/Alpha_c_helix/9'>α-CT chain</scene>), and L2 domains and vertically composed of the FnIII-1, 2, and 3 domains (Figure 1). The insulin receptor's  structural [http://en.wikipedia.org/wiki/Conformational_change conformation change] is what allows it to go from the inactive state to the active state in order to facilitate the autophosphorylation of the tyrosine kinase domain.
 == Relevance ==