Sandbox Reserved 1732: Difference between revisions

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== Structural highlights ==

An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain.

The ~~extracellular~~ domain ~~has~~ a ~~quaternary organization~~.

The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains.

~~When~~ insulin ~~binds to~~ the insulin ~~receptor~~, ~~transmembrane signaling~~ and ~~autophosphorylation~~ of the ~~β-chains at multiple~~ sites ~~is triggered~~.

[[Image:6CE7.png]]

Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Sandbox Reserved 1732: Difference between revisions

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@@ Line 21: / Line 21: @@
 == Structural highlights ==
 An insulin receptor is a dimer of heterodimers. The dimers are noncovalent, but the insulin receptors are covalently maintained as functional dimers by disulfide bonds. An insulin receptor is comprised of 2 α-chains, and 2 β-chains. The α-chain and an estimated 190 residues of the β-chain are located on the extracellular side of the plasma membrane. The rest of the beta-chain consists of a single transmembrane helix, the juxtamembrane domain, and the intracellular tyrosine kinase domain.
-The extracellular domain has a quaternary organization.
+The alpha subunits are the site for insulin binding. Each subunit is comprised of 2 Leucine rich domains (L1 and L2), a Cysteine rich domain (CR) and an α-chain C-terminal helix (α-CT). The two subunits are held together by a disulfide bond between the cysteine rich domains.
-When insulin binds to the insulin receptor, transmembrane signaling and autophosphorylation of the β-chains at multiple sites is triggered.
+[[Image:6CE7.png]]
+Due to the heterodimeric nature of the receptor, there are two types of insulin binding sites that are split into pairs in the alpha subunits: sites 1 and 1' and sites 2 and 2', for a total of 4 binding sites of insulin. Binding sites 1 and 1' have a greater surface area and are more easily accessible for the insulin to bond, resulting in a higher affinity for insulin binding. Binding sites 2 and 2' have less surface area and are located on the back of the beta sheet so their binding sites do not get filled as quickly.
 This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.