[English] 日本語
Yorodumi- PDB-1j2o: Structure of FLIN2, a complex containing the N-terminal LIM domai... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1j2o | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of FLIN2, a complex containing the N-terminal LIM domain of LMO2 and ldb1-LID | ||||||
Components | Fusion of Rhombotin-2 and LIM domain-binding protein 1 | ||||||
Keywords | METAL BINDING PROTEIN / LIM domain / LIM-interaction-domain (LID) | ||||||
Function / homology | Function and homology information regulation of kinase activity / cellular component assembly / negative regulation of erythrocyte differentiation / positive regulation of hemoglobin biosynthetic process / cerebellar Purkinje cell differentiation / epithelial structure maintenance / primitive erythrocyte differentiation / head development / beta-catenin-TCF complex / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery ...regulation of kinase activity / cellular component assembly / negative regulation of erythrocyte differentiation / positive regulation of hemoglobin biosynthetic process / cerebellar Purkinje cell differentiation / epithelial structure maintenance / primitive erythrocyte differentiation / head development / beta-catenin-TCF complex / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / RUNX1 regulates transcription of genes involved in differentiation of HSCs / LIM domain binding / gastrulation with mouth forming second / anterior/posterior axis specification / hair follicle development / embryonic hemopoiesis / regulation of focal adhesion assembly / cell leading edge / somatic stem cell population maintenance / positive regulation of cell adhesion / positive regulation of transcription elongation by RNA polymerase II / regulation of cell migration / cerebellum development / neuron differentiation / RNA polymerase II transcription regulator complex / Wnt signaling pathway / nervous system development / DNA-binding transcription factor binding / transcription regulator complex / transcription coactivator activity / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / cell adhesion / chromatin binding / chromatin / enzyme binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / protein homodimerization activity / protein-containing complex / nucleoplasm / identical protein binding / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, automated noe assignment of ambiguous NOES | ||||||
Authors | Deane, J.E. / Mackay, J.P. / Kwan, A.H. / Sum, E.Y. / Visvader, J.E. / Matthews, J.M. | ||||||
Citation | Journal: EMBO J. / Year: 2003 Title: Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4 Authors: Deane, J.E. / Mackay, J.P. / Kwan, A.H. / Sum, E.Y. / Visvader, J.E. / Matthews, J.M. #1: Journal: PROTEIN ENG. / Year: 2001 Title: Design, production and characterization of FLIN2 and FLIN4: the engineering of intramolecular ldb1:LMO complexes. Authors: Deane, J.E. / Visvader, J.E. / Mackay, J.P. / Matthews, J.M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1j2o.cif.gz | 667 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1j2o.ent.gz | 553.5 KB | Display | PDB format |
PDBx/mmJSON format | 1j2o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1j2o_validation.pdf.gz | 346.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1j2o_full_validation.pdf.gz | 500.9 KB | Display | |
Data in XML | 1j2o_validation.xml.gz | 41.5 KB | Display | |
Data in CIF | 1j2o_validation.cif.gz | 68.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j2/1j2o ftp://data.pdbj.org/pub/pdb/validation_reports/j2/1j2o | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 12604.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Protein is a fusion of the N-terminal LIM domain of LMO2 (residues 26-87) followed by an eleven residue linker (GGSGGHMGSGG) than the LID domain from ldb1 (residues 300-339). Originally ...Details: Protein is a fusion of the N-terminal LIM domain of LMO2 (residues 26-87) followed by an eleven residue linker (GGSGGHMGSGG) than the LID domain from ldb1 (residues 300-339). Originally expressed as a fusion with GST. GST portion removed by treatment with thrombin. Source: (gene. exp.) Mus musculus (house mouse) / Gene: LMO2, Ldb1 / Plasmid: pGEX-2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P25801, UniProt: P70662 |
---|---|
#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||
NMR details | Text: Backbone and Side-chain assignment made using standard 2D and 3D experiments. |
-Sample preparation
Details |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample conditions | pH: 7 / Pressure: ambient / Temperature: 298 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
| ||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: distance geometry, simulated annealing, molecular dynamics, automated noe assignment of ambiguous NOES Software ordinal: 1 Details: The structures are based on 1690 NOE contraints (including 50 ambiguous constraints) and 134 torsion angle restaints | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with favorable non-bond energy Conformers calculated total number: 1000 / Conformers submitted total number: 20 |