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Yorodumi- PDB-4bkf: crystal structure of the human EphA4 ectodomain in complex with h... -
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-Basic information
Entry | Database: PDB / ID: 4bkf | ||||||
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Title | crystal structure of the human EphA4 ectodomain in complex with human ephrinB3 | ||||||
Components |
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Keywords | TRANSFERASE / CELL ADHESION / CELL REPULSION / RECEPTOR CLUSTERING / RECEPTOR CIS INTERACTION / ERYTHROPOETIN-PRODUCING HEPATOCELLULAR RECEPTOR / LBD / SUSHI / EGF / FN | ||||||
Function / homology | Function and homology information axon choice point recognition / trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission / DH domain binding / : / neuron projection fasciculation / positive regulation of Rho guanyl-nucleotide exchange factor activity / corticospinal tract morphogenesis / regulation of astrocyte differentiation / negative regulation of proteolysis involved in protein catabolic process / : ...axon choice point recognition / trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission / DH domain binding / : / neuron projection fasciculation / positive regulation of Rho guanyl-nucleotide exchange factor activity / corticospinal tract morphogenesis / regulation of astrocyte differentiation / negative regulation of proteolysis involved in protein catabolic process / : / neuron projection guidance / nephric duct morphogenesis / regulation of synapse pruning / fasciculation of sensory neuron axon / fasciculation of motor neuron axon / synapse pruning / negative regulation of cellular response to hypoxia / negative regulation of axon regeneration / positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / glial cell migration / negative regulation of axonogenesis / transmembrane-ephrin receptor activity / PH domain binding / GPI-linked ephrin receptor activity / regulation of modification of synaptic structure / negative regulation of epithelial to mesenchymal transition / regulation of dendritic spine morphogenesis / negative regulation of cell adhesion / motor neuron axon guidance / adult walking behavior / adherens junction organization / positive regulation of dendrite morphogenesis / EPH-Ephrin signaling / Ephrin signaling / Somitogenesis / regulation of axonogenesis / positive regulation of amyloid-beta formation / cochlea development / regulation of GTPase activity / EPHA-mediated growth cone collapse / plasma membrane => GO:0005886 / negative regulation of long-term synaptic potentiation / EPH-ephrin mediated repulsion of cells / positive regulation of cell adhesion / ephrin receptor signaling pathway / positive regulation of protein tyrosine kinase activity / axon terminus / axonal growth cone / EPHB-mediated forward signaling / protein tyrosine kinase binding / T cell costimulation / hippocampal mossy fiber to CA3 synapse / ephrin receptor binding / negative regulation of cell migration / dendritic shaft / filopodium / axon guidance / postsynaptic density membrane / adherens junction / Schaffer collateral - CA1 synapse / neuromuscular junction / negative regulation of ERK1 and ERK2 cascade / receptor protein-tyrosine kinase / peptidyl-tyrosine phosphorylation / cellular response to amyloid-beta / negative regulation of neuron projection development / virus receptor activity / cell-cell signaling / presynaptic membrane / nervous system development / amyloid-beta binding / kinase activity / perikaryon / early endosome membrane / protein tyrosine kinase activity / mitochondrial outer membrane / negative regulation of translation / dendritic spine / protein autophosphorylation / protein stabilization / cell adhesion / protein kinase activity / positive regulation of cell migration / axon / dendrite / glutamatergic synapse / positive regulation of cell population proliferation / cell surface / ATP binding / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.65 Å | ||||||
Authors | Seiradake, E. / Schaupp, A. / del Toro Ruiz, D. / Kaufmann, R. / Mitakidis, N. / Harlos, K. / Aricescu, A.R. / Klein, R. / Jones, E.Y. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2013 Title: Structurally Encoded Intraclass Differences in Epha Clusters Drive Distinct Cell Responses Authors: Seiradake, E. / Schaupp, A. / Del Toro Ruiz, D. / Kaufmann, R. / Mitakidis, N. / Harlos, K. / Aricescu, A.R. / Klein, R. / 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 | 4bkf.cif.gz | 526.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4bkf.ent.gz | 441.9 KB | Display | PDB format |
PDBx/mmJSON format | 4bkf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bk/4bkf ftp://data.pdbj.org/pub/pdb/validation_reports/bk/4bkf | HTTPS FTP |
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-Related structure data
Related structure data | 4bk4SC 4bk5C 4bkaC 3d12S 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: 62679.359 Da / Num. of mol.: 2 / Fragment: HEPHA4 ECTODOMAIN, RESIDUES 20-547 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PHLSEC / Cell line (production host): HEK293T / Production host: HOMO SAPIENS (human) References: UniProt: P54764, receptor protein-tyrosine kinase #2: Protein | Mass: 20404.375 Da / Num. of mol.: 2 Fragment: HEPHRINA5 RECEPTOR BINDING DOMAIN, RESIDUES 27-169 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PHLSEC / Cell line (production host): HEK293T / Production host: HOMO SAPIENS (human) / References: UniProt: Q15768 Sequence details | SEQUENCE CORRESPONDS TO HEPHA4 RESIDUES 20-547 FUSED TO AN N-TERMINAL SECRETION SIGNAL SEQUENCE AND ...SEQUENCE CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density % sol: 83.3 % Description: WE USED THE CC CRITERIA TO SELECT THE HIGH RESOLUTION CUT-OFF. THE CC-HALF VALUE IN THE HIGHERST RESOLUTION SHELL IS 16.1. |
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Crystal grow | Details: PROTEIN SAMPLE WAS MIXED 1:1:1 (V/V/V) WITH (0.08 M MAGNESIUM ACETATE TETRAHYDRATE. 0.05 M CACODYLATE PH 6.5, 15% POLYETHYLENE GLYCOL 400) AND 0.1 M SPERMIDINE (HAMPTON). |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength | Wavelength: 0.9173 Å / Relative weight: 1 | |||||||||||||||
Reflection | Resolution: 4.65→106 Å / Num. obs: 25557 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 10.8 % / Biso Wilson estimate: 220.26 Å2 / Rmerge(I) obs: 0.26 / Net I/σ(I): 7.7 | |||||||||||||||
Reflection shell | Resolution: 4.65→4.7 Å / Redundancy: 6.9 % / Mean I/σ(I) obs: 0.5 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRIES 4BK4, 3D12 Resolution: 4.65→106.25 Å / Cor.coef. Fo:Fc: 0.8642 / Cor.coef. Fo:Fc free: 0.9053 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 1.014 Details: ONLY RIGID BODY AND TLS REFIN MOLECULAR REPLACEMENT, DUE TO THE LOW RESOLUTION.
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Displacement parameters | Biso mean: 209.75 Å2
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Refine analyze | Luzzati coordinate error obs: 1.895 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 4.65→106.25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 4.65→4.84 Å / Total num. of bins used: 13
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