Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain.
Identifieur interne : 000085 ( PubMed/Checkpoint ); précédent : 000084; suivant : 000086Higher-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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<Abstract><AbstractText>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.</AbstractText>
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<name sortKey="Lawrence, Michael C" sort="Lawrence, Michael C" uniqKey="Lawrence M" first="Michael C" last="Lawrence">Michael C. Lawrence</name>
<name sortKey="Margetts, Mai B" sort="Margetts, Mai B" uniqKey="Margetts M" first="Mai B" last="Margetts">Mai B. Margetts</name>
<name sortKey="Smith, Brian J" sort="Smith, Brian J" uniqKey="Smith B" first="Brian J" last="Smith">Brian J. Smith</name>
<name sortKey="Ward, Colin W" sort="Ward, Colin W" uniqKey="Ward C" first="Colin W" last="Ward">Colin W. Ward</name>
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<country name="États-Unis"><region name="Ohio"><name sortKey="Whittaker, Jonathan" sort="Whittaker, Jonathan" uniqKey="Whittaker J" first="Jonathan" last="Whittaker">Jonathan Whittaker</name>
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<name sortKey="Weiss, Michael A" sort="Weiss, Michael A" uniqKey="Weiss M" first="Michael A" last="Weiss">Michael A. Weiss</name>
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