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Yorodumi- PDB-1uc6: Solution Structure of the Carboxyl Terminal Domain of the Ciliary... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1uc6 | ||||||
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Title | Solution Structure of the Carboxyl Terminal Domain of the Ciliary Neurotrophic Factor Receptor | ||||||
Components | Ciliary Neurotrophic Factor Receptor alpha | ||||||
Keywords | PROTEIN BINDING / cytokine / ciliary neurotrophic factor / leukemia inhibitory factor / cytokine receptor / fibronectin type III domain-like topology / seven beta-strands / two anti-parallel beta-sheets | ||||||
Function / homology | Function and homology information CNTFR-CLCF1 complex / skeletal muscle organ development / ciliary neurotrophic factor receptor activity / ciliary neurotrophic factor receptor complex / ciliary neurotrophic factor-mediated signaling pathway / brainstem development / sex differentiation / negative regulation of motor neuron apoptotic process / IL-6-type cytokine receptor ligand interactions / cytokine receptor activity ...CNTFR-CLCF1 complex / skeletal muscle organ development / ciliary neurotrophic factor receptor activity / ciliary neurotrophic factor receptor complex / ciliary neurotrophic factor-mediated signaling pathway / brainstem development / sex differentiation / negative regulation of motor neuron apoptotic process / IL-6-type cytokine receptor ligand interactions / cytokine receptor activity / motor neuron apoptotic process / extrinsic component of membrane / cytokine binding / suckling behavior / nervous system development / negative regulation of neuron apoptotic process / apical plasma membrane / external side of plasma membrane / signaling receptor binding / positive regulation of cell population proliferation / signal transduction / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | Man, D. / He, W. / Sze, K.H. / Ke, G. / Smith, D.K. / Ip, N.Y. / Zhu, G. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003 Title: Solution structure of the C-terminal domain of the ciliary neurotrophic factor (CNTF) receptor and ligand free associations among components of the CNTF receptor complex Authors: Man, D. / He, W. / Sze, K.H. / Gong, K. / Smith, D.K. / Zhu, G. / Ip, N.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uc6.cif.gz | 767.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uc6.ent.gz | 654.3 KB | Display | PDB format |
PDBx/mmJSON format | 1uc6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uc/1uc6 ftp://data.pdbj.org/pub/pdb/validation_reports/uc/1uc6 | HTTPS FTP |
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-Related structure data
Similar structure data |
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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 | Mass: 12333.676 Da / Num. of mol.: 1 / Fragment: Carboxyl Terminal Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX-6p1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P26992 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: For determination of hydrogen bonds, amide protons exchanging slowly with deuterons were identified by time course 1H-15N HSQC experiments on a freeze-dried 15N-labelled sample of BC dissolved in D2O buffer. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 100mM NaCl, 10mM sodium phosphate, 0.1mM EDTA pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Following identification of the global fold from manual inspection of the nuclear Overhauser effect spectroscopy data, ambiguous NOE restraints were resolved using the iterative ARIA method ...Details: Following identification of the global fold from manual inspection of the nuclear Overhauser effect spectroscopy data, ambiguous NOE restraints were resolved using the iterative ARIA method (Nilges et al., 1997) and the structure was determined by simulated annealing using the CNS package. | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 21 |