Publikation:

Titin UN2A Acts as a Stable, Non‐Polymorphic Scaffold in its Binding to CARP

Lade...
Vorschaubild

Dateien

Stehle_2-15uqmwh00kk0y6.pdf
Stehle_2-15uqmwh00kk0y6.pdfGröße: 3.68 MBDownloads: 20

Datum

2023

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

ArXiv-ID

Internationale Patentnummer

Link zur Lizenz

Angaben zur Forschungsförderung

Deutsche Forschungsgemeinschaft (DFG): 1154/1-1

Projekt

Open Access-Veröffentlichung
Open Access Hybrid
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

ChemBioChem. Wiley. 2023, 24(19), e202300408. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.202300408

Zusammenfassung

Abstract The N2A segment of titin functions as a pivotal hub for signal transduction and interacts with various proteins involved in structural support, chaperone activities, and transcriptional regulation. Notably, the “unique N2A” (UN2A) subdomain has been shown to interact with the stress‐regulated cardiac ankyrin repeat protein (CARP), which contributes to the regulation of sarcomeric stiffness. Previously, the UN2A domain's three‐dimensional structure was modelled based on its secondary structure content identified by NMR spectroscopy, considering the domain in isolation. In this study, we report experimental long‐range distance distributions by electron paramagnetic resonance (EPR) spectroscopy between the three helixes within the UN2A domain linked to the immunoglobulin domain I81 in the presence and absence of CARP. The data confirm the central three‐helix bundle fold of UN2A and show that this adopts a compact and stable conformation in absence of CARP. After binding to CARP, no significant conformational change was observed, suggesting that the UN2A domain retains its structure upon binding to CARP thereby, mediating the interaction approximately as a rigid‐body.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690STEHLE, Juliane, Jennifer R. FLEMING, Piera-Maria BAUER, Olga MAYANS, Malte DRESCHER, 2023. Titin UN2A Acts as a Stable, Non‐Polymorphic Scaffold in its Binding to CARP. In: ChemBioChem. Wiley. 2023, 24(19), e202300408. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.202300408
BibTex
@article{Stehle2023-08-11Titin-69014,
  year={2023},
  doi={10.1002/cbic.202300408},
  title={Titin UN2A Acts as a Stable, Non‐Polymorphic Scaffold in its Binding to CARP},
  number={19},
  volume={24},
  issn={1439-4227},
  journal={ChemBioChem},
  author={Stehle, Juliane and Fleming, Jennifer R. and Bauer, Piera-Maria and Mayans, Olga and Drescher, Malte},
  note={Article Number: e202300408}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/69014">
    <dc:contributor>Drescher, Malte</dc:contributor>
    <dc:creator>Mayans, Olga</dc:creator>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/69014/1/Stehle_2-15uqmwh00kk0y6.pdf"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2024-01-11T15:17:20Z</dc:date>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Drescher, Malte</dc:creator>
    <dcterms:abstract>Abstract The N2A segment of titin functions as a pivotal hub for signal transduction and interacts with various proteins involved in structural support, chaperone activities, and transcriptional regulation. Notably, the “unique N2A” (UN2A) subdomain has been shown to interact with the stress‐regulated cardiac ankyrin repeat protein (CARP), which contributes to the regulation of sarcomeric stiffness. Previously, the UN2A domain's three‐dimensional structure was modelled based on its secondary structure content identified by NMR spectroscopy, considering the domain in isolation. In this study, we report experimental long‐range distance distributions by electron paramagnetic resonance (EPR) spectroscopy between the three helixes within the UN2A domain linked to the immunoglobulin domain I81 in the presence and absence of CARP. The data confirm the central three‐helix bundle fold of UN2A and show that this adopts a compact and stable conformation in absence of CARP. After binding to CARP, no significant conformational change was observed, suggesting that the UN2A domain retains its structure upon binding to CARP thereby, mediating the interaction approximately as a rigid‐body.</dcterms:abstract>
    <dc:contributor>Fleming, Jennifer R.</dc:contributor>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/69014"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by/4.0/"/>
    <dc:contributor>Stehle, Juliane</dc:contributor>
    <dcterms:title>Titin UN2A Acts as a Stable, Non‐Polymorphic Scaffold in its Binding to CARP</dcterms:title>
    <dcterms:issued>2023-08-11</dcterms:issued>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Stehle, Juliane</dc:creator>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:language>eng</dc:language>
    <dc:contributor>Bauer, Piera-Maria</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/69014/1/Stehle_2-15uqmwh00kk0y6.pdf"/>
    <dc:contributor>Mayans, Olga</dc:contributor>
    <dc:creator>Bauer, Piera-Maria</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2024-01-11T15:17:20Z</dcterms:available>
    <dc:rights>Attribution 4.0 International</dc:rights>
    <dc:creator>Fleming, Jennifer R.</dc:creator>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Ja
Diese Publikation teilen