Sandbox Reserved 1732: Difference between revisions

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<Structure load='6SOF' size='400' frame='true' align='right' caption='Insulin Receptor' scene='Insert optional scene name here' />
<Structure load='6SOF' size='400' frame='true' align='right' caption='Insulin Receptor' scene='Insert optional scene name here' />
<scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene>
<scene name='91/919041/Insulin_receptor/1'>Text To Be Displayed</scene>
==Insulin Receptor Structure ==
<StructureSection load='6SOF' size='350' side='right' caption='Alpha Chain of Insulin Receptor' scene=''>
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 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.


Alpha Chain
Alpha Chain
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