Publikation: Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
The repurposing of structurally conserved protein domains in different functional contexts is thought to be a driving force in the evolution of complex protein interaction networks. The BTB/POZ domain is such a versatile binding module that occurs over 200 times in the human proteome with diverse protein-specific adaptations. In BTB-zinc-finger transcription factors, the BTB domain drives homo- and heterodimerization as well as interactions with non-BTB-domain-containing proteins. Which mechanisms encode specificity in these interactions at a structural level is incompletely understood. Here, we uncover an atypical peptide-binding site in the BTB domain of the MYC-interacting zinc-finger protein 1 (MIZ1) that arises from local flexibility of the core BTB fold and may provide a target site for MIZ1-directed therapeutic approaches. Intriguingly, the identified binding mode requires the BTB domain to be in a homodimeric state, thus holding opportunities for functional discrimination between homo- and heterodimers of MIZ1 in the cell.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
ORTH, Barbara, Bodo SANDER, Andreas MÖGLICH, Kay DIEDERICHS, Martin EILERS, Sonja LORENZ, 2021. Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1. In: Structure. Cell Press. 2021, 29(11), pp. 1230-1240.e5. ISSN 0969-2126. eISSN 1878-4186. Available under: doi: 10.1016/j.str.2021.06.005BibTex
@article{Orth2021-11-04Ident-54181, year={2021}, doi={10.1016/j.str.2021.06.005}, title={Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1}, number={11}, volume={29}, issn={0969-2126}, journal={Structure}, pages={1230--1240.e5}, author={Orth, Barbara and Sander, Bodo and Möglich, Andreas and Diederichs, Kay and Eilers, Martin and Lorenz, Sonja} }
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/123456789/54181"> <dc:creator>Sander, Bodo</dc:creator> <dc:creator>Orth, Barbara</dc:creator> <dcterms:issued>2021-11-04</dcterms:issued> <dc:creator>Eilers, Martin</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/54181"/> <dc:rights>terms-of-use</dc:rights> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2021-07-05T07:08:16Z</dcterms:available> <dc:creator>Diederichs, Kay</dc:creator> <dc:contributor>Lorenz, Sonja</dc:contributor> <dc:creator>Möglich, Andreas</dc:creator> <dcterms:abstract xml:lang="eng">The repurposing of structurally conserved protein domains in different functional contexts is thought to be a driving force in the evolution of complex protein interaction networks. The BTB/POZ domain is such a versatile binding module that occurs over 200 times in the human proteome with diverse protein-specific adaptations. In BTB-zinc-finger transcription factors, the BTB domain drives homo- and heterodimerization as well as interactions with non-BTB-domain-containing proteins. Which mechanisms encode specificity in these interactions at a structural level is incompletely understood. Here, we uncover an atypical peptide-binding site in the BTB domain of the MYC-interacting zinc-finger protein 1 (MIZ1) that arises from local flexibility of the core BTB fold and may provide a target site for MIZ1-directed therapeutic approaches. Intriguingly, the identified binding mode requires the BTB domain to be in a homodimeric state, thus holding opportunities for functional discrimination between homo- and heterodimers of MIZ1 in the cell.</dcterms:abstract> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:contributor>Orth, Barbara</dc:contributor> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Diederichs, Kay</dc:contributor> <dc:contributor>Möglich, Andreas</dc:contributor> <dc:contributor>Eilers, Martin</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2021-07-05T07:08:16Z</dc:date> <dc:language>eng</dc:language> <dc:creator>Lorenz, Sonja</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dc:contributor>Sander, Bodo</dc:contributor> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <dcterms:title>Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1</dcterms:title> </rdf:Description> </rdf:RDF>