|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
histone H3-K4 acetylation / cellular component assembly / negative regulation of erythrocyte differentiation / mesendoderm development / regulation of kinase activity / positive regulation of hemoglobin biosynthetic process / cerebellar Purkinje cell differentiation / head development / epithelial structure maintenance / primitive erythrocyte differentiation ...histone H3-K4 acetylation / cellular component assembly / negative regulation of erythrocyte differentiation / mesendoderm development / regulation of kinase activity / positive regulation of hemoglobin biosynthetic process / cerebellar Purkinje cell differentiation / head development / epithelial structure maintenance / primitive erythrocyte differentiation / bHLH transcription factor binding / beta-catenin-TCF complex / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / regulation of transcription elongation by RNA polymerase II / RUNX1 regulates transcription of genes involved in differentiation of HSCs / LIM domain binding / gastrulation with mouth forming second / anterior/posterior axis specification / cellular response to thyroid hormone stimulus / regulation of focal adhesion assembly / embryonic hemopoiesis / cell leading edge / somatic stem cell population maintenance / hair follicle development / positive regulation of cell adhesion / cerebellum development / regulation of cell migration / transcription coregulator binding / neuron differentiation / Wnt signaling pathway / RNA polymerase II transcription regulator complex / protein self-association / nervous system development / DNA-binding transcription factor binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription regulator complex / transcription by RNA polymerase II / transcription coactivator activity / cell differentiation / cell adhesion / negative regulation of DNA-templated transcription / chromatin / chromatin binding / negative regulation of transcription by RNA polymerase II / enzyme binding / positive regulation of transcription by RNA polymerase II / protein homodimerization activity / protein-containing complex / nucleoplasm / metal ion binding / identical protein binding / nucleus
Similarity search - Function
LIM-domain binding protein/SEUSS / LIM interaction domain / LIM-domain binding protein / LIM interaction domain (LID) / LIM interaction domain (LID) domain profile. / Cysteine Rich Protein / Cysteine Rich Protein / LIM zinc-binding domain signature. / LIM domain / Zinc-binding domain present in Lin-11, Isl-1, Mec-3. ...LIM-domain binding protein/SEUSS / LIM interaction domain / LIM-domain binding protein / LIM interaction domain (LID) / LIM interaction domain (LID) domain profile. / Cysteine Rich Protein / Cysteine Rich Protein / LIM zinc-binding domain signature. / LIM domain / Zinc-binding domain present in Lin-11, Isl-1, Mec-3. / Zinc finger, LIM-type / LIM domain profile. / Ribbon / Mainly Beta
Similarity search - Domain/homology
Rhombotin-2 / LIM domain-binding protein 1
Similarity search - Component
|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.|
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.
|Structure viewer||Molecule: |
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|PDBx/mmCIF format||1j2o.cif.gz||663.4 KB||Display||PDBx/mmCIF format|
|PDB format||pdb1j2o.ent.gz||572.3 KB||Display||PDB format|
|PDBx/mmJSON format||1j2o.json.gz||Tree view||PDBx/mmJSON format|
|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|
-Related structure data
|Related structure data|
C: citing same article (ref.)
|Similar structure data|
|PDB pages||PDBj / wwPDB / NCBI|
|Related items in Molecule of the Month|
A: Fusion of Rhombotin-2 and LIM domain-binding protein 1
|#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
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: Backbone and Side-chain assignment made using standard 2D and 3D experiments.|
|Sample conditions||pH: 7.0 / Pressure: ambient / Temperature: 298 K|
*PLUSMethod: other / Details: NMR
|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|
|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
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