+Open data
-Basic information
Entry | Database: PDB / ID: 2joc | ||||||
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Title | Mouse Itch 3rd domain phosphorylated in T30 | ||||||
Components | Itchy E3 ubiquitin protein ligase | ||||||
Keywords | LIGASE / Itch / WW / Phosphothreonine | ||||||
Function / homology | Function and homology information regulation of protein deubiquitination / Downregulation of ERBB4 signaling / negative regulation of cytoplasmic pattern recognition receptor signaling pathway / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of necroptotic cell death / negative regulation of defense response to virus / Degradation of GLI1 by the proteasome / protein K29-linked ubiquitination / Hedgehog 'on' state / T cell anergy ...regulation of protein deubiquitination / Downregulation of ERBB4 signaling / negative regulation of cytoplasmic pattern recognition receptor signaling pathway / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of necroptotic cell death / negative regulation of defense response to virus / Degradation of GLI1 by the proteasome / protein K29-linked ubiquitination / Hedgehog 'on' state / T cell anergy / positive regulation of T cell anergy / RUNX1 regulates transcription of genes involved in differentiation of HSCs / CXCR chemokine receptor binding / CD4-positive, alpha-beta T cell proliferation / NOD1/2 Signaling Pathway / Antigen processing: Ubiquitination & Proteasome degradation / negative regulation of CD4-positive, alpha-beta T cell proliferation / negative regulation of JNK cascade / HECT-type E3 ubiquitin transferase / arrestin family protein binding / positive regulation of receptor catabolic process / negative regulation of NF-kappaB transcription factor activity / ubiquitin-like protein ligase binding / protein monoubiquitination / protein K63-linked ubiquitination / ligase activity / protein autoubiquitination / protein K48-linked ubiquitination / ribonucleoprotein complex binding / ubiquitin ligase complex / protein catabolic process / receptor internalization / protein polyubiquitination / positive regulation of protein catabolic process / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / cell cortex / early endosome membrane / cytoplasmic vesicle / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / defense response to virus / protein ubiquitination / intracellular membrane-bounded organelle / innate immune response / apoptotic process / negative regulation of apoptotic process / protein-containing complex / nucleoplasm / membrane / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Authors | Macias, M.J. / Shaw, A.Z. / Martin-Malpartida, P. / Morales, B. / Ruiz, L. / Ramirez-Espain, X. / Yraola, F. / Royo, M. | ||||||
Citation | Journal: Structure / Year: 2007 Title: NMR Structural Studies of the ItchWW3 Domain Reveal that Phosphorylation at T30 Inhibits the Interaction with PPxY-Containing Ligands Authors: Morales, B. / Ramirez-Espain, X. / Shaw, A.Z. / Martin-Malpartida, P. / Yraola, F. / Sanchez-Tillo, E. / Farrera, C. / Celada, A. / Royo, M. / 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 | 2joc.cif.gz | 90.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2joc.ent.gz | 70.4 KB | Display | PDB format |
PDBx/mmJSON format | 2joc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jo/2joc ftp://data.pdbj.org/pub/pdb/validation_reports/jo/2joc | 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: 4356.688 Da / Num. of mol.: 1 / Fragment: WW 3 domain, sequence database residues 399-432 / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of the peptide is naturally found in Mus musculus (mouse). References: UniProt: Q8C863, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.0 mM PhosphoI3, 20 mM Sodium Phosphate, 100 mM NaCl, 0.02% v/v Sodium Azide, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | |||||||||||||||
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Sample |
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 7 / Conformers submitted total number: 7 |