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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Croll</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, QLD 4059, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute of Health and Biomedical Innovation, Queensland University of Technology, QLD 4059</wicri:regionArea><wicri:noRegion>QLD 4059</wicri:noRegion></affiliation></author><author><name sortKey="Smith, Brian J" sort="Smith, Brian J" uniqKey="Smith B" first="Brian J" last="Smith">Brian J. 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Weiss</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry, Case Western Reserve University, Cleveland, OH 44106, USA; Departments of Physiology, and Biomedical Engineering, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Case Western Reserve University, Cleveland, OH 44106, USA; Departments of Physiology, and Biomedical Engineering, Case Western Reserve University, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Ward, Colin W" sort="Ward, Colin W" uniqKey="Ward C" first="Colin W" last="Ward">Colin W. Ward</name><affiliation wicri:level="1"><nlm:affiliation>Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052</wicri:regionArea><wicri:noRegion>VIC 3052</wicri:noRegion></affiliation></author><author><name sortKey="Lawrence, Michael C" sort="Lawrence, Michael C" uniqKey="Lawrence M" first="Michael C" last="Lawrence">Michael C. Lawrence</name><affiliation wicri:level="1"><nlm:affiliation>Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC 3010, Australia. Electronic address: lawrence@wehi.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC 3010</wicri:regionArea><wicri:noRegion>VIC 3010</wicri:noRegion></affiliation></author></analytic><series><title level="j">Structure (London, England : 1993)</title><idno type="eISSN">1878-4186</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>Australie</li><li>États-Unis</li></country><region><li>Ohio</li></region></list><tree><country name="Australie"><noRegion><name sortKey="Croll, Tristan I" sort="Croll, Tristan I" uniqKey="Croll T" first="Tristan I" last="Croll">Tristan I. Croll</name></noRegion><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></country><country name="États-Unis"><region name="Ohio"><name sortKey="Whittaker, Jonathan" sort="Whittaker, Jonathan" uniqKey="Whittaker J" first="Jonathan" last="Whittaker">Jonathan Whittaker</name></region><name sortKey="Weiss, Michael A" sort="Weiss, Michael A" uniqKey="Weiss M" first="Michael A" last="Weiss">Michael A. Weiss</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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