Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain.
Identifieur interne : 000177 ( Main/Exploration ); précédent : 000176; suivant : 000178Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain.
Auteurs : Tristan I. Croll [Australie] ; Brian J. Smith [Australie] ; Mai B. Margetts [Australie] ; Jonathan Whittaker [États-Unis] ; Michael A. Weiss [États-Unis] ; Colin W. Ward [Australie] ; Michael C. Lawrence [Australie]Source :
- Structure (London, England : 1993) [ 1878-4186 ] ; 2016.
Abstract
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.
DOI: 10.1016/j.str.2015.12.014
PubMed: 26853939
Affiliations:
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<front><div type="abstract" xml:lang="en">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.</div>
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