Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain
By T. Croll, Brian J. Smith, M. Margetts, J. Whittaker, M. Weiss, Colin W. Ward, M. Lawrence. 2016
136 citations recorded by the source corpus.
SUMMARY Insulin receptor (IR) signaling is critical to controlling nutrient uptake and metabolism. However, only a low-resolution (3.8 Å) 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 Å 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.
Subfields: Endocrinology, Diabetes and Metabolism, Molecular Biology, Surgery
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Endocrinology, Diabetes and Metabolism
In Molecular Biology
In Surgery
Citations in the corpus
- ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps (2018, methodology): “Recently, I demonstrated the use of interactive MDFF simulations to improve models built into challenging low-resolution crystallographic maps (Croll et al., 2016; Croll & Andersen, 2016; Focht et al., 2017).”