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Open data
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Basic information
Entry | Database: PDB / ID: 1yzb | ||||||
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Title | Solution structure of the Josephin domain of Ataxin-3 | ||||||
![]() | Machado-Joseph disease protein 1![]() | ||||||
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Function / homology | ![]() protein localization to cytosolic proteasome complex / regulation of cell-substrate adhesion / positive regulation of ERAD pathway / monoubiquitinated protein deubiquitination / intermediate filament cytoskeleton organization / protein K48-linked deubiquitination / nuclear inclusion body / positive regulation of ubiquitin-dependent protein catabolic process / protein K63-linked deubiquitination / cellular response to misfolded protein ...protein localization to cytosolic proteasome complex / regulation of cell-substrate adhesion / positive regulation of ERAD pathway / monoubiquitinated protein deubiquitination / intermediate filament cytoskeleton organization / protein K48-linked deubiquitination / nuclear inclusion body / positive regulation of ubiquitin-dependent protein catabolic process / protein K63-linked deubiquitination / cellular response to misfolded protein / K48-linked deubiquitinase activity / K63-linked deubiquitinase activity / protein quality control for misfolded or incompletely synthesized proteins / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / negative regulation of TORC1 signaling / cellular response to amino acid starvation / Josephin domain DUBs / nucleotide-excision repair / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Nicastro, G. / Masino, L. / Menon, R.P. / Knowles, P.P. / McDonald, N.Q. / Pastore, A. | ||||||
![]() | ![]() Title: The solution structure of the Josephin domain of ataxin-3: Structural determinants for molecular recognition Authors: Nicastro, G. / Menon, R.P. / Masino, L. / Knowles, P.P. / McDonald, N.Q. / Pastore, A. #1: Journal: J.Biomol.Nmr / Year: 2004 Title: Assignment of the 1H, 13C, and 15N resonances of the Josephin domain of human ataxin-3 Authors: Nicastro, G. / Masino, L. / Frenkiel, T.A. / Kelly, G. / McCormick, J. / Menon, R.P. / Pastore, A. #2: Journal: J.Mol.Biol. / Year: 2004 Title: Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3 Authors: Masino, L. / Nicastro, G. / Menon, R.P. / Dal Piaz, F. / Calder, L. / Pastore, A. #3: Journal: Febs Lett. / Year: 2003 Title: Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail Authors: Masino, L. / Musi, V. / Menon, R.P. / Fusi, P. / Kelly, G. / Frenkiel, T.A. / Trottier, Y. / Pastore, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 568.3 KB | Display | ![]() |
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PDB format | ![]() | 473.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | ![]() Mass: 21053.768 Da / Num. of mol.: 1 / Fragment: N-terminal domain of Ataxin-3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy |
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Sample preparation
Details | Contents: 0.4mM of Josephin 15N, 13C; 20mM sodium phosphate buffer (pH 6.5); 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 20mM sodium phosphate / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: ![]() Details: the structures are based on a total of 5532 unambiguous and 927 ambiguous restraints, 114 dihedral angle restraints, 44 distance restraints from hydrogen bonds. | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |