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Yorodumi- PDB-1u38: Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1u38 | ||||||
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Title | Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains | ||||||
Components |
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Keywords | PROTEIN TRANSPORT / X11s/Mints / PDZ domain / scaffold protein / protein trafficking | ||||||
Function / homology | Function and homology information gamma-aminobutyric acid secretion / Dopamine Neurotransmitter Release Cycle / glutamate secretion / axo-dendritic transport / Assembly and cell surface presentation of NMDA receptors / Neurexins and neuroligins / presynaptic active zone membrane / presynaptic modulation of chemical synaptic transmission / locomotory behavior / intracellular protein transport ...gamma-aminobutyric acid secretion / Dopamine Neurotransmitter Release Cycle / glutamate secretion / axo-dendritic transport / Assembly and cell surface presentation of NMDA receptors / Neurexins and neuroligins / presynaptic active zone membrane / presynaptic modulation of chemical synaptic transmission / locomotory behavior / intracellular protein transport / Schaffer collateral - CA1 synapse / multicellular organism growth / synaptic vesicle / nervous system development / amyloid-beta binding / regulation of gene expression / protein-containing complex assembly / chemical synaptic transmission / in utero embryonic development / dendritic spine / cell adhesion / glutamatergic synapse / perinuclear region of cytoplasm / Golgi apparatus / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model type details | minimized average | ||||||
Authors | Feng, W. / Long, J.-F. / Chan, L.-N. / He, C. / Fu, A. / Xia, J. / Ip, N.Y. / Zhang, M. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2005 Title: Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem Authors: Long, J.-F. / Feng, W. / Wang, R. / Chan, L.-N. / Ip, F.C. / Xia, J. / Ip, N.Y. / Zhang, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1u38.cif.gz | 565.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1u38.ent.gz | 470.3 KB | Display | PDB format |
PDBx/mmJSON format | 1u38.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1u38_validation.pdf.gz | 355.4 KB | Display | wwPDB validaton report |
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Full document | 1u38_full_validation.pdf.gz | 586.5 KB | Display | |
Data in XML | 1u38_validation.xml.gz | 42.4 KB | Display | |
Data in CIF | 1u38_validation.cif.gz | 67 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/u3/1u38 ftp://data.pdbj.org/pub/pdb/validation_reports/u3/1u38 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9557.253 Da / Num. of mol.: 1 / Fragment: PDZ1 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET32a / Production host: Escherichia coli (E. coli) / References: UniProt: Q02410 |
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#2: Protein/peptide | Mass: 490.592 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic peptide / References: GenBank: 22035548 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 100mM potassium phosphate / pH: 6.5 / Pressure: 1 atm / Temperature: 303 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 750 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |