Molecular Mechanism of STIL Coiled-Coil Domain Oligomerization.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
27 Sep 2023
Historique:
received: 20 08 2023
revised: 16 09 2023
accepted: 21 09 2023
medline: 2 11 2023
pubmed: 14 10 2023
entrez: 14 10 2023
Statut: epublish

Résumé

Coiled-coil domains (CCDs) play key roles in regulating both healthy cellular processes and the pathogenesis of various diseases by controlling protein self-association and protein-protein interactions. Here, we probe the mechanism of oligomerization of a peptide representing the CCD of the STIL protein, a tetrameric multi-domain protein that is over-expressed in several cancers and associated with metastatic spread. STIL tetramerization is mediated both by an intrinsically disordered domain (STIL

Identifiants

pubmed: 37834064
pii: ijms241914616
doi: 10.3390/ijms241914616
pmc: PMC10572602
pii:
doi:

Substances chimiques

Peptides 0
Proteins 0
STIL protein, human 0
Intracellular Signaling Peptides and Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

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Auteurs

Mai Shamir (M)

Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus Givat Ram, Jerusalem 91904, Israel.

Freddie J O Martin (FJO)

School of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TS, UK.

Derek N Woolfson (DN)

School of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TS, UK.
School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Bristol BioDesign Institute, University of Bristol, Cantock's Close, Bristol BS8 1TS, UK.

Assaf Friedler (A)

Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus Givat Ram, Jerusalem 91904, Israel.

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Classifications MeSH