User:R. Jeremy Johnson/Insulin Receptor: Difference between revisions

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===Subunit Organization===

The alpha and beta subunits of the extracellular domains fold over one another and form a <scene name='83/839263/V_shape/3'>"V" shape</scene> when the insulin receptor is inactivated. Upon activation, the extracellular domain undergoes a conformational change and forms a <scene name='83/839263/T-shape/4'>"T" shape</scene>. An additional component to the [http://en.wikipedia.org/wiki/Ectodomain ectodomain] is <scene name='83/839263/Alpha-ct/2'> α-CT</scene>.<ref name= "Uchikawa" /> Each of the dimers has an α-CT. The α-CT is a single alpha-helix ~~and it~~ plays an important role in insulin binding and stabilization of the "T" shape activated conformation. ~~The~~ α-CT interacts with a leucine-rich region of the alpha subunit and a fibronectin type III region of the beta subunit to form the insulin binding sites known as <scene name='83/839263/Insulin_molecules_at_site_1/1'>site 1 and site 1'</scene>.<ref name="Uchikawa" />

The alpha and beta subunits of the extracellular domains fold over one another and form a <scene name='83/839263/V_shape/3'>"V" shape</scene> when the insulin receptor is inactivated. Upon activation, the extracellular domain undergoes a conformational change and forms a <scene name='83/839263/T-shape/4'>"T" shape</scene>. An additional component to the [http://en.wikipedia.org/wiki/Ectodomain ectodomain] is <scene name='83/839263/Alpha-ct/2'> α-CT</scene>.<ref name= "Uchikawa" /> Each of the dimers has an α-CT helix. The α-CT helix is a single alpha-helix that plays an important role in insulin binding and stabilization of the "T" shape activated conformation. α-CT interacts with a leucine-rich region of the alpha subunit and a fibronectin type III region of the beta subunit to form the insulin binding sites known as <scene name='83/839263/Insulin_molecules_at_site_1/1'>site 1 and site 1'</scene>.<ref name="Uchikawa" />

The structure of the extracellular domain is stabilized through multiple [http://en.wikipedia.org/wiki/Disulfide disulfide bonds]. The alpha subunits are linked through two disulfide bonds, with the main one being between <scene name='83/839263/Cys_holding_alphas_together/4'>Cys524</scene> of two adjacent alpha subuntis <ref name="Schäffer" />. <scene name='83/839263/Cys_683_holding_alphas_togethe/3'>Cys683</scene> of both alpha subunits are also held together with a disulfide bond.<ref name="Sparrow"> PMID: 9368005</ref> The alpha subunit is also attached to the beta subunit by a disulfide bond between the <scene name='83/839263/Alpha_beta_link_by_disulfide/5'>Cys647 of the alpha subunit and Cys872 of the beta subunit</scene>.<ref name="Sparrow" />

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 ===Subunit Organization===
-The alpha and beta subunits of the extracellular domains fold over one another and form a <scene name='83/839263/V_shape/3'>"V" shape</scene> when the insulin receptor is inactivated. Upon activation, the extracellular domain undergoes a conformational change and forms a <scene name='83/839263/T-shape/4'>"T" shape</scene>. An additional component to the [http://en.wikipedia.org/wiki/Ectodomain ectodomain] is <scene name='83/839263/Alpha-ct/2'> α-CT</scene>.<ref name= "Uchikawa" /> Each of the dimers has an α-CT. The α-CT is a single alpha-helix and it plays an important role in insulin binding and stabilization of the "T" shape activated conformation. The α-CT interacts with a leucine-rich region of the alpha subunit and a fibronectin type III region of the beta subunit to form the insulin binding sites known as <scene name='83/839263/Insulin_molecules_at_site_1/1'>site 1 and site 1'</scene>.<ref name="Uchikawa" />
+The alpha and beta subunits of the extracellular domains fold over one another and form a <scene name='83/839263/V_shape/3'>"V" shape</scene> when the insulin receptor is inactivated. Upon activation, the extracellular domain undergoes a conformational change and forms a <scene name='83/839263/T-shape/4'>"T" shape</scene>. An additional component to the [http://en.wikipedia.org/wiki/Ectodomain ectodomain] is <scene name='83/839263/Alpha-ct/2'> α-CT</scene>.<ref name= "Uchikawa" /> Each of the dimers has an α-CT helix. The α-CT helix is a single alpha-helix that plays an important role in insulin binding and stabilization of the "T" shape activated conformation. α-CT interacts with a leucine-rich region of the alpha subunit and a fibronectin type III region of the beta subunit to form the insulin binding sites known as <scene name='83/839263/Insulin_molecules_at_site_1/1'>site 1 and site 1'</scene>.<ref name="Uchikawa" />
 The structure of the extracellular domain is stabilized through multiple [http://en.wikipedia.org/wiki/Disulfide disulfide bonds]. The alpha subunits are linked through two disulfide bonds, with the main one being between <scene name='83/839263/Cys_holding_alphas_together/4'>Cys524</scene> of two adjacent alpha subuntis <ref name="Schäffer" />. <scene name='83/839263/Cys_683_holding_alphas_togethe/3'>Cys683</scene> of both alpha subunits  are also held together with a disulfide bond.<ref name="Sparrow"> PMID: 9368005</ref> The alpha subunit is also attached to the beta subunit by a disulfide bond between the <scene name='83/839263/Alpha_beta_link_by_disulfide/5'>Cys647 of the alpha subunit and Cys872 of the beta subunit</scene>.<ref name="Sparrow" />