ArticleMolecules (Basel, Switzerland)2013
Structure of the C-terminal region of the Frizzled receptor 1 in detergent micelles.
Article in Molecules (Basel, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Molecular evolutionary and structural analysis of familial exudative vitreoretinopathy associated FZD4 gene.BMC evolutionary biology · 2019Article
- Biophysical and functional characterization of Norrin signaling through Frizzled4.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mutational analysis of hepatitis E virus ORF1 "Y-domain": Effects on RNA replication and virion infectivity.World journal of gastroenterology · 2017Article
- Essential role of the Dishevelled DEP domain in a Wnt-dependent human-cell-based complementation assay.Journal of cell science · 2016Article
- Frizzled-4 C-terminus Distal to KTXXXW Motif is Essential for Normal Dishevelled Recruitment and Norrin-stimulated Activation of Lef/Tcf-dependent Transcriptional Activation.Journal of molecular signaling · 2016Article
- Solution structure of the transmembrane domain of the mouse erythropoietin receptor in detergent micelles.Scientific reports · 2015Article
- Structural insight into the transmembrane domain and the juxtamembrane region of the erythropoietin receptor in micelles.Biophysical journal · 2014Article
- WNT/Frizzled signalling: receptor-ligand selectivity with focus on FZD-G protein signalling and its physiological relevance: IUPHAR Review 3.British journal of pharmacology · 2014Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The C-terminal domains of the Frizzleds (FZDs) contain a short conserved motif (KTXXXW). It has been demonstrated that FZDs interacted with the PDZ domain of the cytoplasmic proteins such as Dishevelled through this motif and mutations in this motif disrupted Wnt/β-catenin signaling. We carried out structural studies for a peptide derived from the C-terminal domain of the FZD1 in different solvents using circular dichroism and solution NMR spectroscopy. Our results showed that this domain was unstructured in an aqueous solution and formed a helical structure in detergent micelles. Fluorescence studies suggested that the tryptophan residue (W630) in the motif interacted with micelles. The solution structure of the peptide in sodium dodecyl sulfate micelles was determined and an amphipathic helix was identified. This helix may have similar function to the helix 8 of other G protein-coupled receptors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.