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The insulin receptor is a [http://en.wikipedia.org/wiki/Transmembrane_protein transmembrane] receptor <ref name="De Meyts"/> that resides in the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] and is activated by the binding of insulin. The insulin receptor belongs to the large class of [http://en.wikipedia.org/wiki/Receptor_tyrosine_kinase receptor tyrosine kinase] (RTKs). RTKs are found at the cell surface and have a high affinity for a particular ligand. RTKs are made up of three distinct parts: an extracellular domain with ligand binding sites, a transmembrane region, and an intracellular domain with the tyrosine kinases that initiate intracellular signaling cascades <ref name="De Meyts"> PMID: 27512793 </ref>. Downstream signaling from the insulin receptor initiates a variety of cellular pathways including glucose [http://en.wikipedia.org/wiki/Homeostasis homeostasis], regulation of lipid, protein, and carbohydrate metabolism, gene expression, and even modulation of brain neurotransmitter levels <ref name="Tatulian"/>. '''This page focuses specifically on the insulin receptor's role in glucose homeostasis.''' Through recent cryo-EM structures of the insulin receptor bound in various conformations, a complete three-dimensional understanding of this conformational changes in finally coming into focus. The discussion on this page will include an explanation of the insulin receptors' structure that lends to its ability go through a unique conformation change in induce signaling, as well as highlight the functionalities of the receptors' multiple binding sites.