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Yorodumi- PDB-5fww: Wnt modulator Kremen in complex with DKK1 (CRD2) and LRP6 (PE3PE4) -
+Open data
-Basic information
Entry | Database: PDB / ID: 5fww | ||||||
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Title | Wnt modulator Kremen in complex with DKK1 (CRD2) and LRP6 (PE3PE4) | ||||||
Components |
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Keywords | SIGNALING PROTEIN / WNT / CELL SURFACE / SIGNALLING / MEMBRANE PROTEIN | ||||||
Function / homology | Function and homology information negative regulation of mesodermal cell fate specification / regulation of endodermal cell fate specification / positive regulation of Wnt signaling pathway, calcium modulating pathway / Wnt signaling pathway involved in somitogenesis / negative regulation of Wnt-Frizzled-LRP5/6 complex assembly / positive regulation of midbrain dopaminergic neuron differentiation / negative regulation of presynapse assembly / Signaling by LRP5 mutants / regulation of dopaminergic neuron differentiation / Wnt-Frizzled-LRP5/6 complex ...negative regulation of mesodermal cell fate specification / regulation of endodermal cell fate specification / positive regulation of Wnt signaling pathway, calcium modulating pathway / Wnt signaling pathway involved in somitogenesis / negative regulation of Wnt-Frizzled-LRP5/6 complex assembly / positive regulation of midbrain dopaminergic neuron differentiation / negative regulation of presynapse assembly / Signaling by LRP5 mutants / regulation of dopaminergic neuron differentiation / Wnt-Frizzled-LRP5/6 complex / negative regulation of cardiac muscle cell differentiation / motor learning / Negative regulation of TCF-dependent signaling by WNT ligand antagonists / endoderm formation / synapse pruning / neural crest formation / Signaling by RNF43 mutants / endocardial cushion development / negative regulation of axon regeneration / heart induction / regulation of receptor internalization / receptor antagonist activity / kinase inhibitor activity / toxin transmembrane transporter activity / Wnt receptor activity / low-density lipoprotein particle receptor activity / co-receptor binding / positive regulation of Wnt signaling pathway, planar cell polarity pathway / Wnt-protein binding / midbrain dopaminergic neuron differentiation / cellular response to cholesterol / cell communication / negative regulation of protein serine/threonine kinase activity / dopaminergic neuron differentiation / heart valve development / frizzled binding / negative regulation of ossification / Wnt signalosome / regulation of canonical Wnt signaling pathway / Disassembly of the destruction complex and recruitment of AXIN to the membrane / embryonic limb morphogenesis / neural crest cell differentiation / limb development / face morphogenesis / low-density lipoprotein particle receptor binding / negative regulation of SMAD protein signal transduction / negative regulation of Wnt signaling pathway / negative regulation of peptidyl-serine phosphorylation / negative regulation of smooth muscle cell apoptotic process / mesoderm formation / negative regulation of BMP signaling pathway / hair follicle development / canonical Wnt signaling pathway / coreceptor activity / positive regulation of cell cycle / response to retinoic acid / regulation of neuron apoptotic process / forebrain development / regulation of synaptic transmission, glutamatergic / Regulation of FZD by ubiquitination / negative regulation of protein binding / protein localization to plasma membrane / TCF dependent signaling in response to WNT / positive regulation of JNK cascade / positive regulation of DNA-binding transcription factor activity / growth factor activity / negative regulation of canonical Wnt signaling pathway / cell morphogenesis / Wnt signaling pathway / response to peptide hormone / cell-cell adhesion / endocytosis / negative regulation of neuron projection development / nervous system development / positive regulation of cytosolic calcium ion concentration / early endosome membrane / cytoplasmic vesicle / chemical synaptic transmission / learning or memory / membrane raft / signaling receptor binding / neuronal cell body / synapse / positive regulation of gene expression / negative regulation of apoptotic process / apoptotic process / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / cell surface / endoplasmic reticulum / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 3.5 Å | ||||||
Authors | Zebisch, M. / Jackson, V.A. / Jones, E.Y. | ||||||
Citation | Journal: Structure / Year: 2016 Title: Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight Into Ternary Complex Formation with Lrp6 and Dickkopf Authors: Zebisch, M. / Jackson, V.A. / Zhao, Y. / Jones, E.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5fww.cif.gz | 206 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5fww.ent.gz | 160.4 KB | Display | PDB format |
PDBx/mmJSON format | 5fww.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5fww_validation.pdf.gz | 438.4 KB | Display | wwPDB validaton report |
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Full document | 5fww_full_validation.pdf.gz | 439.2 KB | Display | |
Data in XML | 5fww_validation.xml.gz | 35.7 KB | Display | |
Data in CIF | 5fww_validation.cif.gz | 47 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fw/5fww ftp://data.pdbj.org/pub/pdb/validation_reports/fw/5fww | HTTPS FTP |
-Related 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: 70093.898 Da / Num. of mol.: 1 / Fragment: PE3PE4, RESIDUES 630-1246 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Gene: LRP6 / Plasmid: PHLSEC / Cell line (production host): HEK293 / Production host: HOMO SAPIENS (human) / References: UniProt: O75581 |
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#2: Protein | Mass: 32728.531 Da / Num. of mol.: 1 / Fragment: ECD, RESIDUES 30-322 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Gene: KREMEN1, KREMEN, KRM1 / Plasmid: PHLSEC / Cell line (production host): HEK293 / Production host: HOMO SAPIENS (human) / References: UniProt: Q96MU8 |
#3: Protein | Mass: 9607.076 Da / Num. of mol.: 1 / Fragment: CRD2, RESIDUES 182-266 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Gene: DKK1, UNQ492/PRO1008 / Plasmid: PHLSEC / Cell line (production host): HEK293 / Production host: HOMO SAPIENS (human) / References: UniProt: O94907 |
#4: Chemical | ChemComp-CA / |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.3 % / Description: NONE |
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Crystal grow | pH: 7.5 / Details: 20 %W/V PEG3350 0.2 M NA/K-PHOSPHATE, pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 |
Detector | Type: DECTRIS PILATUS / Detector: PIXEL / Date: Sep 15, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→67.68 Å / Num. obs: 8070 / % possible obs: 51.6 % / Observed criterion σ(I): -3 / Redundancy: 3.9 % / Rmerge(I) obs: 0.37 / Net I/σ(I): 4.6 |
-Processing
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Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 3.5→135.36 Å / Cor.coef. Fo:Fc: 0.763 / Cor.coef. Fo:Fc free: 0.701 / Cross valid method: THROUGHOUT / ESU R Free: 1.576 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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: 58.615 Å2
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Refinement step | Cycle: LAST / Resolution: 3.5→135.36 Å
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