Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain.
Identifieur interne : 000110 ( PubMed/Curation ); précédent : 000109; suivant : 000111Higher-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
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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></affiliation></author><author><name sortKey="Smith, Brian J" sort="Smith, Brian J" uniqKey="Smith B" first="Brian J" last="Smith">Brian J. Smith</name><affiliation wicri:level="1"><nlm:affiliation>La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086</wicri:regionArea></affiliation></author><author><name sortKey="Margetts, Mai B" sort="Margetts, Mai B" uniqKey="Margetts M" first="Mai B" last="Margetts">Mai B. Margetts</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></affiliation></author><author><name sortKey="Whittaker, Jonathan" sort="Whittaker, Jonathan" uniqKey="Whittaker J" first="Jonathan" last="Whittaker">Jonathan Whittaker</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, 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</wicri:regionArea></affiliation></author><author><name sortKey="Weiss, Michael A" sort="Weiss, Michael A" uniqKey="Weiss M" first="Michael A" last="Weiss">Michael A. Weiss</name><affiliation wicri:level="1"><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></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></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></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><pubmed><MedlineCitation Owner="NLM" Status="In-Data-Review"><PMID Version="1">26853939</PMID><DateCreated><Year>2016</Year><Month>03</Month><Day>03</Day></DateCreated><DateRevised><Year>2016</Year><Month>05</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-4186</ISSN><JournalIssue CitedMedium="Internet"><Volume>24</Volume><Issue>3</Issue><PubDate><Year>2016</Year><Month>Mar</Month><Day>1</Day></PubDate></JournalIssue><Title>Structure (London, England : 1993)</Title><ISOAbbreviation>Structure</ISOAbbreviation></Journal><ArticleTitle>Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain.</ArticleTitle><Pagination><MedlinePgn>469-76</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.str.2015.12.014</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0969-2126(16)00007-1</ELocationID><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><CopyrightInformation>Copyright © 2016 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Croll</LastName><ForeName>Tristan I</ForeName><Initials>TI</Initials><AffiliationInfo><Affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, QLD 4059, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Smith</LastName><ForeName>Brian J</ForeName><Initials>BJ</Initials><AffiliationInfo><Affiliation>La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Margetts</LastName><ForeName>Mai B</ForeName><Initials>MB</Initials><AffiliationInfo><Affiliation>Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Whittaker</LastName><ForeName>Jonathan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Case Western Reserve University, Cleveland, OH 44106, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Weiss</LastName><ForeName>Michael A</ForeName><Initials>MA</Initials><AffiliationInfo><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.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ward</LastName><ForeName>Colin W</ForeName><Initials>CW</Initials><AffiliationInfo><Affiliation>Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lawrence</LastName><ForeName>Michael C</ForeName><Initials>MC</Initials><AffiliationInfo><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. 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