Johnson's Monday Lab Sandbox for Insulin Receptor
From Proteopedia
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The insulin receptor resides within the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] of insulin targeted cells of various organs and tissues, including the liver, skeletal muscle, and adipose. The insulin receptor is activated by insulin molecules binding. Once activated, the receptor serves as the gateway for the regulation of various cellular processes. These processes include but are not limited to glucose transport, glycogen storage, [http://en.wikipedia.org/wiki/Autophagy autophagy], [http://en.wikipedia.org/wiki/Apoptosis apoptosis], and gene expression. Additionally, problems with the insulin receptor has been associated with the development of diseases such as Alzheimer's, type II diabetes, and cancer <ref name="Scapin" />. Characterization of the structure of the insulin receptor, as well as understanding of the molecular mechanisms, which initiate a [http://en.wikipedia.org/wiki/Conformational_change conformational change], are important for understanding the role that the insulin receptor plays within a cell and in the development of the disease. | The insulin receptor resides within the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] of insulin targeted cells of various organs and tissues, including the liver, skeletal muscle, and adipose. The insulin receptor is activated by insulin molecules binding. Once activated, the receptor serves as the gateway for the regulation of various cellular processes. These processes include but are not limited to glucose transport, glycogen storage, [http://en.wikipedia.org/wiki/Autophagy autophagy], [http://en.wikipedia.org/wiki/Apoptosis apoptosis], and gene expression. Additionally, problems with the insulin receptor has been associated with the development of diseases such as Alzheimer's, type II diabetes, and cancer <ref name="Scapin" />. Characterization of the structure of the insulin receptor, as well as understanding of the molecular mechanisms, which initiate a [http://en.wikipedia.org/wiki/Conformational_change conformational change], are important for understanding the role that the insulin receptor plays within a cell and in the development of the disease. | ||
==Insulin== | ==Insulin== | ||
| - | [[Image:Insulin.png|thumb|right|150px|Figure 1: Insulin molecule]] <scene name='83/839263/Insulin_molecule/3'> | + | [[Image:Insulin.png|thumb|right|150px|Figure 1: Insulin molecule]] The <scene name='83/839263/Insulin_molecule/3'>insulin molecule</scene> is a [http://en.wikipedia.org/wiki/Hormone hormone made of two seperate amino acid chains that is synthesized and secreted from the [http://en.wikipedia.org/wiki/Pancreatic_islets islets of Langerhans] of the pancreas in response to high concentrations of glucose in the blood. Once it is secreted, insulin moves through the bloodstream and binds to unactivated insulin receptors residing in the plasma membrane. The receptor is fully activated after multiple insulin molecules are bound, and as previously mentioned, the regulation of various cellular processes is initiated. |
==Structure== | ==Structure== | ||
The insulin receptor is a [http://en.wikipedia.org/wiki/Receptor_tyrosine_kinase receptor tyrosine kinase]. It is a [http://en.wikipedia.org/wiki/Heterotetramer heterotetramer] that is constructed from two [http://en.wiktionary.org/wiki/homodimer homodimers]. Each homodimer maintains an extracellular domain, transmembrane helix, and an intracellular domain. The insulin is divided into <scene name='83/839263/Alpha_and_beta_subunit/3'>alpha and beta</scene> [http://en.wikipedia.org/wiki/Protein_subunit subunits]. The alpha subunit is characterized by two leucine-rich regions and one cysteine-rich region. The beta subunit contains three fibronectin type III domains along with the transmembrane domain and intracellular tyrosine kinase domain that could not be shown in one continous PDB structure. 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>. | The insulin receptor is a [http://en.wikipedia.org/wiki/Receptor_tyrosine_kinase receptor tyrosine kinase]. It is a [http://en.wikipedia.org/wiki/Heterotetramer heterotetramer] that is constructed from two [http://en.wiktionary.org/wiki/homodimer homodimers]. Each homodimer maintains an extracellular domain, transmembrane helix, and an intracellular domain. The insulin is divided into <scene name='83/839263/Alpha_and_beta_subunit/3'>alpha and beta</scene> [http://en.wikipedia.org/wiki/Protein_subunit subunits]. The alpha subunit is characterized by two leucine-rich regions and one cysteine-rich region. The beta subunit contains three fibronectin type III domains along with the transmembrane domain and intracellular tyrosine kinase domain that could not be shown in one continous PDB structure. 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>. | ||
Revision as of 02:05, 17 April 2020
Insulin Receptor
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