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Yorodumi- PDB-1bp3: THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bp3 | ||||||
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Title | THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX | ||||||
Components |
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Keywords | HORMONE/GROWTH FACTOR / HORMONE / RECEPTOR / HORMONE-GROWTH FACTOR complex | ||||||
Function / homology | Function and homology information growth hormone activity / prolactin receptor activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / positive regulation of growth / regulation of epithelial cell differentiation / animal organ development / cell surface receptor signaling pathway via STAT / prostate gland growth ...growth hormone activity / prolactin receptor activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / positive regulation of growth / regulation of epithelial cell differentiation / animal organ development / cell surface receptor signaling pathway via STAT / prostate gland growth / mammary gland epithelial cell differentiation / steroid biosynthetic process / activation of Janus kinase activity / cellular response to granulocyte macrophage colony-stimulating factor stimulus / positive regulation of multicellular organism growth / positive regulation of D-glucose transmembrane transport / positive regulation of insulin-like growth factor receptor signaling pathway / growth hormone receptor binding / activation of transmembrane receptor protein tyrosine kinase activity / growth hormone receptor signaling pathway / Prolactin receptor signaling / cytokine binding / peptide hormone binding / cell surface receptor signaling pathway via JAK-STAT / Synthesis, secretion, and deacylation of Ghrelin / mammary gland alveolus development / growth hormone receptor signaling pathway via JAK-STAT / regulation of cell adhesion / positive regulation of tyrosine phosphorylation of STAT protein / Growth hormone receptor signaling / positive regulation of B cell proliferation / positive regulation of protein autophosphorylation / lactation / embryo implantation / response to nutrient levels / cytokine activity / endosome lumen / positive regulation of receptor signaling pathway via JAK-STAT / response to bacterium / growth factor activity / positive regulation of MAP kinase activity / hormone activity / cytokine-mediated signaling pathway / positive regulation of cold-induced thermogenesis / response to estradiol / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / external side of plasma membrane / lipid binding / positive regulation of cell population proliferation / negative regulation of apoptotic process / protein kinase binding / cell surface / extracellular space / extracellular region / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å | ||||||
Authors | Somers, W. / Ultsch, M. / De Vos, A.M. / Kossiakoff, A.A. | ||||||
Citation | Journal: Nature / Year: 1994 Title: The X-ray structure of a growth hormone-prolactin receptor complex. Authors: Somers, W. / Ultsch, M. / De Vos, A.M. / Kossiakoff, A.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bp3.cif.gz | 92 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bp3.ent.gz | 68.2 KB | Display | PDB format |
PDBx/mmJSON format | 1bp3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bp3_validation.pdf.gz | 379.3 KB | Display | wwPDB validaton report |
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Full document | 1bp3_full_validation.pdf.gz | 419.6 KB | Display | |
Data in XML | 1bp3_validation.xml.gz | 14 KB | Display | |
Data in CIF | 1bp3_validation.cif.gz | 19.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bp/1bp3 ftp://data.pdbj.org/pub/pdb/validation_reports/bp/1bp3 | HTTPS FTP |
-Related structure data
Related structure data | 1a22S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 22252.135 Da / Num. of mol.: 1 / Mutation: G120R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P01241 |
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#2: Protein | Mass: 24543.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P16471 |
#3: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 9 |
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-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.57 % |
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Crystal grow | pH: 6 / Details: pH 6.00 |
-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 0.908 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.908 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→10 Å / Num. obs: 9883 / % possible obs: 93 % / Rmerge(I) obs: 0.108 |
Reflection shell | Resolution: 2.9→3 Å / % possible all: 89 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1A22 Resolution: 2.9→10 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.9→10 Å
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Refine LS restraints |
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