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- W2405465246 endingPage "5532" @default.
- W2405465246 startingPage "5523" @default.
- W2405465246 abstract "The insulin receptor (IR) is a (αβ)2-type transmembrane tyrosine kinase that plays a central role in cell metabolism. Each αβ heterodimer consists of an extracellular ligand-binding α-subunit and a membrane-spanning β-subunit that comprises the cytoplasmic tyrosine kinase (TK) domain and the phosphorylation sites. The α- and β-subunits are linked via a single disulfide bridge, and the (αβ)2 tetramer is formed by disulfide bonds between the α-chains. Insulin binding induces conformational changes in IR that reach the intracellular β-subunit followed by a protein phosphorylation and activation cascade. Defects in this signaling process, including IR dysfunction caused by mutations, result in type 2 diabetes. Rational drug design aimed at treatment of diabetes relies on knowledge of the detailed structure of IR and the dynamic structural transformations during transmembrane signaling. Recent X-ray crystallographic studies have provided important clues about the mode of binding of insulin to IR, the resulting structural changes and their transmission to the TK domain, but a complete understanding of the structural basis underlying insulin signaling has not been achieved. This review presents a critical analysis of the current status of the structure-function relationship of IR, with a comparative assessment of the other IR family receptors, and discusses potential advancements that may provide insight into the molecular mechanism of insulin signaling." @default.
- W2405465246 created "2016-06-24" @default.
- W2405465246 creator A5068810331 @default.
- W2405465246 date "2015-09-03" @default.
- W2405465246 modified "2023-10-01" @default.
- W2405465246 title "Structural Dynamics of Insulin Receptor and Transmembrane Signaling" @default.
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- W2405465246 doi "https://doi.org/10.1021/acs.biochem.5b00805" @default.
- W2405465246 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26322622" @default.