Journal
STRUCTURE
Volume 24, Issue 3, Pages 469-476Publisher
CELL PRESS
DOI: 10.1016/j.str.2015.12.014
Keywords
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Funding
- National Health and Medical Research Council [1005896, 1058233]
- Hazel and Pip Appel Fund
- National Institutes of Health [R01 DK040949]
- Australian Synchrotron Research Program
- Commonwealth of Australia's Major National Research Facilities Program
- Sanofi (Germany)
- National Health and Medical Research Council of Australia [1058233] Funding Source: NHMRC
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Insulin receptor (IR) signaling is critical to controlling nutrient uptake and metabolism. However, only a low-resolution (3.8 angstrom) 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 angstrom 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.
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