ArticleScientific reports2015
Solution structure of the transmembrane domain of the mouse erythropoietin receptor in detergent micelles.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Structural Modeling of Cytokine-Receptor-JAK2 Signaling Complexes Using AlphaFold Multimer.Journal of chemical information and modeling · 2023Article
- Structural modeling of cytokine-receptor-JAK2 signaling complexes using AlphaFold Multimer.bioRxiv : the preprint server for biology · 2023Article
- Second-generation non-hematopoietic erythropoietin-derived peptide for neuroprotection.Redox biology · 2022Article
- Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles.International journal of molecular sciences · 2022Article
- Orchestration of signaling by structural disorder in class 1 cytokine receptors.Cell communication and signaling : CCS · 2020Article
- Transmembrane Protein Aptamer Induces Cooperative Signaling by the EPO Receptor and the Cytokine Receptor β-Common Subunit.iScience · 2019Article
- Computational analysis of ligand-receptor interactions in wild-type and mutant erythropoietin complexes.Advances and applications in bioinformatics and chemistry : AABC · 2018Article
- Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions.eLife · 2017Article
- Solution NMR Spectroscopy in Target-Based Drug Discovery.Molecules (Basel, Switzerland) · 2017Review
- Rethinking JAK2 inhibition: towards novel strategies of more specific and versatile Janus kinase inhibition.Leukemia · 2017Review
- Do All X-ray Structures of Protein-Ligand Complexes Represent Functional States? EPOR, a Case Study.Biophysical journal · 2017Article
- A combined computational and structural model of the full-length human prolactin receptor.Nature communications · 2016Article
- Structure of the transmembrane domain of human nicastrin-a component of γ-secretase.Scientific reports · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Erythropoiesis is regulated by the erythropoietin receptor (EpoR) binding to its ligand. The transmembrane domain (TMD) and the juxtamembrane (JM) regions of the EpoR are important for signal transduction across the cell membrane. We report a solution NMR study of the mouse erythropoietin receptor (mEpoR) comprising the TMD and the JM regions reconstituted in dodecylphosphocholine (DPC) micelles. The TMD and the C-terminal JM region of the mEpoR are mainly α-helical, adopting a similar structure to those of the human EpoR. Residues from S216 to T219 in mEpoR form a short helix. Relaxation study demonstrates that the TMD of the mEpoR is rigid whilst the N-terminal region preceding the TMD is flexible. Fluorescence spectroscopy and sequence analysis indicate that the C-terminal JM region is exposed to the solvent. Helix wheel result shows that there is hydrophilic patch in the TMD of the mEpoR formed by residues S231, S238 and T242, and these residues might be important for the receptor dimerization.
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