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Structure of the human insulin receptor ectodomain, IRDeltabeta construct, in complex with four Fab moleculesStructure of the human insulin receptor ectodomain, IRDeltabeta construct, in complex with four Fab molecules
Structural highlights
FunctionPublication Abstract from PubMedInsulin receptor (IR) signaling is critical to controlling nutrient uptake and metabolism. However, only a low-resolution (3.8 A) structure currently exists for the IR ectodomain, with some segments ill-defined or unmodeled due to disorder. Here, we revise this structure using new diffraction data to 3.3 A resolution that allow improved modeling of the N-linked glycans, the first and third fibronectin type III domains, and the insert domain. A novel haptic interactive molecular dynamics strategy was used to aid fitting to low-resolution electron density maps. The resulting model provides a foundation for investigation of structural transitions in IR upon ligand binding. Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain.,Croll TI, Smith BJ, Margetts MB, Whittaker J, Weiss MA, Ward CW, Lawrence MC Structure. 2016 Jan 27. pii: S0969-2126(16)00007-1. doi:, 10.1016/j.str.2015.12.014. PMID:26853939[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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