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Yorodumi- PDB-4nxr: Crystal Structure of T-cell Lymphoma Invasion and Metastasis-1 PD... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4nxr | ||||||
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Title | Crystal Structure of T-cell Lymphoma Invasion and Metastasis-1 PDZ Domain Quadruple Mutant (QM) in Complex With Neurexin-1 Peptide | ||||||
Components |
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Keywords | signaling Protein/Peptide / Beta barrel fold protein / PDZ domain / peptide binding / specificity mutant / scaffold signaling protein for cell adhesion and cell junction / signaling domain / signaling Protein-Peptide complex | ||||||
Function / homology | Function and homology information positive regulation of Schwann cell chemotaxis / regulation of non-canonical Wnt signaling pathway / regulation of dopaminergic neuron differentiation / extrinsic component of postsynaptic density membrane / neuroligin family protein binding / Activated NTRK2 signals through CDK5 / neuron cell-cell adhesion / regulation of epithelial to mesenchymal transition / positive regulation of dendritic spine morphogenesis / regulation of insulin secretion involved in cellular response to glucose stimulus ...positive regulation of Schwann cell chemotaxis / regulation of non-canonical Wnt signaling pathway / regulation of dopaminergic neuron differentiation / extrinsic component of postsynaptic density membrane / neuroligin family protein binding / Activated NTRK2 signals through CDK5 / neuron cell-cell adhesion / regulation of epithelial to mesenchymal transition / positive regulation of dendritic spine morphogenesis / regulation of insulin secretion involved in cellular response to glucose stimulus / regulation of modification of postsynaptic actin cytoskeleton / cell-cell contact zone / protein localization to membrane / cardiac muscle hypertrophy / activation of GTPase activity / Neurexins and neuroligins / Wnt signaling pathway, planar cell polarity pathway / regulation of small GTPase mediated signal transduction / main axon / neuron projection extension / small GTPase-mediated signal transduction / positive regulation of axonogenesis / NRAGE signals death through JNK / Rac protein signal transduction / CDC42 GTPase cycle / EPH-ephrin mediated repulsion of cells / RHOA GTPase cycle / positive regulation of epithelial to mesenchymal transition / RAC3 GTPase cycle / RAC2 GTPase cycle / ephrin receptor signaling pathway / axonal growth cone / RAC1 GTPase cycle / EPHB-mediated forward signaling / cell adhesion molecule binding / guanyl-nucleotide exchange factor activity / cell-matrix adhesion / regulation of ERK1 and ERK2 cascade / response to cocaine / receptor tyrosine kinase binding / ruffle membrane / kinase binding / G alpha (12/13) signalling events / cell-cell junction / cell migration / transmembrane signaling receptor activity / positive regulation of protein binding / microtubule binding / protein-containing complex assembly / microtubule / dendritic spine / membrane => GO:0016020 / positive regulation of cell migration / neuronal cell body / glutamatergic synapse / lipid binding / synapse / positive regulation of cell population proliferation / signal transduction / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Liu, X. / Speckhard, D.C. / Shepherd, T.R. / Hengel, S.R. / Fuentes, E.J. | ||||||
Citation | Journal: Structure / Year: 2016 Title: Distinct Roles for Conformational Dynamics in Protein-Ligand Interactions. Authors: Liu, X. / Speckhard, D.C. / Shepherd, T.R. / Sun, Y.J. / Hengel, S.R. / Yu, L. / Fowler, C.A. / Gakhar, L. / Fuentes, E.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4nxr.cif.gz | 36.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4nxr.ent.gz | 23.8 KB | Display | PDB format |
PDBx/mmJSON format | 4nxr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nx/4nxr ftp://data.pdbj.org/pub/pdb/validation_reports/nx/4nxr | HTTPS FTP |
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-Related structure data
Related structure data | 4nxpC 4nxqC 3kzdS S: Starting model for refinement C: citing same article (ref.) |
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Similar 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: 10192.402 Da / Num. of mol.: 1 / Fragment: PDZ domain / Mutation: L911M, K912E, L915F, L920V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Strain: human / Gene: TIAM1 / Plasmid: PET21A-6HIS-rTEV / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q13009 |
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#2: Protein/peptide | Mass: 1060.158 Da / Num. of mol.: 1 / Fragment: UNP residue 659-666 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P58401 |
#3: Chemical | ChemComp-EPE / |
#4: Chemical | ChemComp-ANS / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.83 Å3/Da / Density % sol: 32.61 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: 0.1M Sodium acetate, 0.1M HEPES, pH=7.5, 22% PEG 4000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 1 Å |
Detector | Type: NOIR-1 / Detector: CCD / Date: Dec 14, 2012 |
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→39.06 Å / Num. obs: 6821 / % possible obs: 98.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Biso Wilson estimate: 11.4 Å2 / Rmerge(I) obs: 0.033 / Net I/σ(I): 39.7 |
Reflection shell | Resolution: 1.9→1.94 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.035 / Mean I/σ(I) obs: 11 / % possible all: 87.1 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 3KZD Resolution: 1.9→39.06 Å / SU ML: 0.15 / σ(F): 0.64 / Phase error: 18.87 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→39.06 Å
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Refine LS restraints |
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LS refinement shell |
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