+Open data
-Basic information
Entry | Database: PDB / ID: 2jup | ||||||
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Title | FBP28WW2 domain in complex with the PPLIPPPP peptide | ||||||
Components |
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Keywords | TRANSCRIPTION / FBP28WW domain / PPLIPPPP peptide / Alternative splicing / Coiled coil / Nucleus / Polymorphism / Repressor / Transcription regulation / Actin-binding / Cell junction / Cytoplasm / Membrane / Phosphorylation | ||||||
Function / homology | Function and homology information ureteric bud invasion / forelimb morphogenesis / mRNA Splicing - Major Pathway / hindlimb morphogenesis / actin nucleation / positive regulation of actin nucleation / proline-rich region binding / ubiquitin-like protein conjugating enzyme binding / RNA polymerase binding / skeletal system morphogenesis ...ureteric bud invasion / forelimb morphogenesis / mRNA Splicing - Major Pathway / hindlimb morphogenesis / actin nucleation / positive regulation of actin nucleation / proline-rich region binding / ubiquitin-like protein conjugating enzyme binding / RNA polymerase binding / skeletal system morphogenesis / limb development / positive regulation of actin filament polymerization / positive regulation of focal adhesion assembly / RNA splicing / actin filament / transcription coregulator activity / adherens junction / mRNA processing / SH3 domain binding / transcription corepressor activity / gene expression / actin binding / microtubule binding / RNA polymerase II-specific DNA-binding transcription factor binding / DNA-binding transcription factor activity / DNA-templated transcription / endoplasmic reticulum membrane / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / nucleoplasm / identical protein binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) synthetic construct (others) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Authors | Ramirez-Espain, X. / Ruiz, L. / Martin-Malpartida, P. / Oschkinat, H. / Macias, M.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structural Characterization of a New Binding Motif and a Novel Binding Mode in Group 2 WW Domains Authors: Ramirez-Espain, X. / Ruiz, L. / Martin-Malpartida, P. / Oschkinat, H. / Macias, M.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jup.cif.gz | 148.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jup.ent.gz | 121.6 KB | Display | PDB format |
PDBx/mmJSON format | 2jup.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ju/2jup ftp://data.pdbj.org/pub/pdb/validation_reports/ju/2jup | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4364.709 Da / Num. of mol.: 1 / Fragment: WW 2 domain, sequence database residues 430-466 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tcerg1, Taf2s / Production host: Escherichia coli (E. coli) / References: UniProt: Q8CGF7 |
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#2: Protein/peptide | Mass: 884.071 Da / Num. of mol.: 1 / Fragment: sequence database residues, 881-888 / Source method: obtained synthetically Details: The authors state that the peptide was chemically synthesized and the sequence corresponds to the mouse formin protein. Source: (synth.) synthetic construct (others) / References: UniProt: Q05860 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.100 / pH: 5.8 / Pressure: ambient / Temperature: 285 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 | |||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 60 / Conformers submitted total number: 10 |