+Open data
-Basic information
Entry | Database: PDB / ID: 1t2m | ||||||
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Title | Solution Structure Of The Pdz Domain Of AF-6 | ||||||
Components | AF-6 protein | ||||||
Keywords | PROTEIN BINDING / Chromosomal translocation / Proto-oncogene | ||||||
Function / homology | Function and homology information positive regulation of cell-cell adhesion mediated by cadherin / establishment of protein localization to plasma membrane / establishment of endothelial intestinal barrier / positive regulation of cell-cell adhesion / pore complex assembly / cell-cell adhesion mediated by cadherin / bicellular tight junction assembly / cell-cell contact zone / Adherens junctions interactions / tight junction ...positive regulation of cell-cell adhesion mediated by cadherin / establishment of protein localization to plasma membrane / establishment of endothelial intestinal barrier / positive regulation of cell-cell adhesion / pore complex assembly / cell-cell adhesion mediated by cadherin / bicellular tight junction assembly / cell-cell contact zone / Adherens junctions interactions / tight junction / pore complex / cell adhesion molecule binding / negative regulation of cell migration / adherens junction / small GTPase binding / regulation of protein localization / actin filament binding / cell-cell junction / cell junction / cell-cell signaling / cell adhesion / nuclear speck / cadherin binding / positive regulation of gene expression / signal transduction / nucleoplasm / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Authors | Zhou, H. / Wu, J.H. / Xu, Y.Q. / Huang, A.D. / Shi, Y.Y. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Solution Structure of AF-6 PDZ Domain and Its Interaction with the C-terminal Peptides from Neurexin and Bcr Authors: Zhou, H. / Xu, Y. / Yang, Y. / Huang, A. / Wu, J. / Shi, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t2m.cif.gz | 530.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t2m.ent.gz | 444.6 KB | Display | PDB format |
PDBx/mmJSON format | 1t2m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t2/1t2m ftp://data.pdbj.org/pub/pdb/validation_reports/t2/1t2m | 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: 10637.198 Da / Num. of mol.: 1 / Fragment: Pdz domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Tissue: brain / Plasmid: pET-22b(+) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P55196 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: structure was determined using triple-resonance NMR spectroscopy |
-Sample preparation
Details | Contents: 50mM phosphate buffer NA; 1mM EDTA; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50mM phosphate, 1mM EDTA / pH: 5.9 / Pressure: 1 atm / 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 | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 Details: The structure was also refined with CSI version 1.0 (authors: David S. Wishart) | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |