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- PDB-3d48: Crystal structure of a prolactin receptor antagonist bound to the... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3d48 | ||||||
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Title | Crystal structure of a prolactin receptor antagonist bound to the extracellular domain of the prolactin receptor | ||||||
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![]() | Hormone/Hormone Receptor / Cytokine-Cytokine Receptor Complex / Four-helix Bundle / Glycoprotein / Hormone / Lactation / Secreted / Alternative splicing / Membrane / Receptor / Transmembrane / Hormone-Hormone Receptor COMPLEX | ||||||
Function / homology | ![]() prolactin receptor activity / prolactin receptor binding / positive regulation of lactation / regulation of epithelial cell differentiation / prolactin signaling pathway / prostate gland growth / mammary gland epithelial cell differentiation / mammary gland development / steroid biosynthetic process / activation of Janus kinase activity ...prolactin receptor activity / prolactin receptor binding / positive regulation of lactation / regulation of epithelial cell differentiation / prolactin signaling pathway / prostate gland growth / mammary gland epithelial cell differentiation / mammary gland development / steroid biosynthetic process / activation of Janus kinase activity / cellular response to granulocyte macrophage colony-stimulating factor stimulus / activation of transmembrane receptor protein tyrosine kinase activity / Prolactin receptor signaling / cytokine binding / negative regulation of endothelial cell proliferation / peptide hormone binding / cell surface receptor signaling pathway via JAK-STAT / mammary gland alveolus development / regulation of cell adhesion / Growth hormone receptor signaling / positive regulation of B cell proliferation / positive regulation of protein autophosphorylation / lactation / embryo implantation / negative regulation of angiogenesis / response to nutrient levels / endosome lumen / female pregnancy / response to bacterium / positive regulation of receptor signaling pathway via JAK-STAT / hormone activity / cytokine-mediated signaling pathway / positive regulation of miRNA transcription / positive regulation of cold-induced thermogenesis / positive regulation of canonical NF-kappaB signal transduction / cell surface receptor signaling pathway / receptor complex / Amyloid fiber formation / 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 | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Svensson, L.A. / Breinholt, J. | ||||||
![]() | ![]() Title: Crystal structure of a prolactin receptor antagonist bound to the extracellular domain of the prolactin receptor Authors: Svensson, L.A. / Bondensgaard, K. / Norskov-Lauritsen, L. / Christensen, L. / Becker, P. / Andersen, M.D. / Maltesen, M.J. / Rand, K.D. / Breinholt, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.4 KB | Display | ![]() |
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PDB format | ![]() | 68.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 457.5 KB | Display | ![]() |
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Full document | ![]() | 470.3 KB | Display | |
Data in XML | ![]() | 17.7 KB | Display | |
Data in CIF | ![]() | 24.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bp3S ![]() 1f6fS ![]() 1n9d ![]() 1rw5S S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 21948.000 Da / Num. of mol.: 1 / Fragment: residues 12-199 / Mutation: Q12S, G129R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Protein | Mass: 24529.850 Da / Num. of mol.: 1 / Fragment: Extracellular Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
#3: Chemical | ChemComp-CO3 / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.41 Å3/Da / Density % sol: 63.9 % |
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Crystal grow | Temperature: 297 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 3.5M Sodium Chloride, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 18, 2007 |
Radiation | Monochromator: DOUBLE-CRYSTAL MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. all: 21763 / Num. obs: 21797 / % possible obs: 99.8 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 11.2 % / Biso Wilson estimate: 46.4 Å2 / Rsym value: 0.083 / Net I/σ(I): 22.46 |
Reflection shell | Resolution: 2.5→2.56 Å / Redundancy: 11.2 % / Mean I/σ(I) obs: 5.5 / Num. unique all: 21797 / Rsym value: 0.501 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: FOR THE R CHAIN, PDB ENTRY 1BP3. FOR THE P CHAIN, A CORE OF A MODELER HOMOLOGY MODEL BASED ON PDB ENTRIES 1BP3, 1F6F, 1RW5 AND 1N9D. Resolution: 2.5→20 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.863 / WRfactor Rfree: 0.29 / WRfactor Rwork: 0.212 / SU B: 9.77 / SU ML: 0.222 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.335 / ESU R Free: 0.289 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.307 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20
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