+Open data
-Basic information
Entry | Database: PDB / ID: 5oek | ||||||
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Title | Putative active dimeric state of GHR transmembrane domain | ||||||
Components | Growth hormone receptor | ||||||
Keywords | MEMBRANE PROTEIN / Dimer / GHR / Growth hormone receptor / Homodimer / Human / Receptor / Transmembrane domain / Tyrosine kinase | ||||||
Function / homology | Function and homology information growth hormone receptor activity / regulation of response to nutrient levels / growth hormone receptor complex / taurine metabolic process / response to gravity / cartilage development involved in endochondral bone morphogenesis / positive regulation of multicellular organism growth / hormone metabolic process / proline-rich region binding / growth hormone receptor signaling pathway ...growth hormone receptor activity / regulation of response to nutrient levels / growth hormone receptor complex / taurine metabolic process / response to gravity / cartilage development involved in endochondral bone morphogenesis / positive regulation of multicellular organism growth / hormone metabolic process / proline-rich region binding / growth hormone receptor signaling pathway / response to food / response to cycloheximide / growth factor binding / Prolactin receptor signaling / cytokine binding / peptide hormone binding / cell surface receptor signaling pathway via JAK-STAT / regulation of multicellular organism growth / positive regulation of tyrosine phosphorylation of STAT protein / response to glucocorticoid / Growth hormone receptor signaling / cellular response to hormone stimulus / hormone-mediated signaling pathway / SH2 domain binding / response to interleukin-1 / insulin-like growth factor receptor signaling pathway / positive regulation of cell differentiation / positive regulation of receptor signaling pathway via JAK-STAT / positive regulation of MAP kinase activity / receptor internalization / cytokine-mediated signaling pathway / cytoplasmic ribonucleoprotein granule / cellular response to insulin stimulus / endocytosis / positive regulation of peptidyl-tyrosine phosphorylation / response to estradiol / protein phosphatase binding / receptor complex / external side of plasma membrane / neuronal cell body / lipid binding / protein kinase binding / cell surface / protein homodimerization activity / extracellular space / extracellular region / identical protein binding / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Lesovoy, D.M. / Bocharov, E.V. / Bocharova, O.V. / Urban, A.S. / Arseniev, A.S. | ||||||
Funding support | Russian Federation, 1items
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Citation | Journal: Biochim. Biophys. Acta / Year: 2018 Title: Structural basis of the signal transduction via transmembrane domain of the human growth hormone receptor. Authors: Bocharov, E.V. / Lesovoy, D.M. / Bocharova, O.V. / Urban, A.S. / Pavlov, K.V. / Volynsky, P.E. / Efremov, R.G. / Arseniev, A.S. #1: Journal: Bioorg. Khim. / Year: 2015 Title: Preparation of Transmembrane Fragments Growth Hormone Receptor GHR in a Cell-Free Expression System for Structural Studies. Authors: Bocharova, O.V. / Kuzmichev, P.K. / Urban, A.S. / Goncharuk, S.A. / Bocharov, E.V. / Arsenyev, A.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5oek.cif.gz | 568.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5oek.ent.gz | 480.4 KB | Display | PDB format |
PDBx/mmJSON format | 5oek.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5oek_validation.pdf.gz | 343.1 KB | Display | wwPDB validaton report |
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Full document | 5oek_full_validation.pdf.gz | 603.9 KB | Display | |
Data in XML | 5oek_validation.xml.gz | 27.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oe/5oek ftp://data.pdbj.org/pub/pdb/validation_reports/oe/5oek | HTTPS FTP |
-Related structure data
Related structure data | 5ohdC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 5145.129 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: The author sequence numbering corresponds to the Swiss-Prot annotation of the human Growth hormone receptor (GHR), P10912 Source: (gene. exp.) Homo sapiens (human) / Gene: GHR Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) Strain (production host): BL21(DE3) / References: UniProt: P10912 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
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