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Yorodumi- PDB-1klq: The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Confo... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1klq | ||||||
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Title | The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon Binding to Either Mad1 or Cdc20 | ||||||
Components |
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Keywords | CELL CYCLE / protein-peptide complex / MAD2 FAMILY | ||||||
Function / homology | Function and homology information mitotic spindle assembly checkpoint MAD1-MAD2 complex / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of mitotic cell cycle spindle assembly checkpoint / establishment of centrosome localization / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / nuclear pore nuclear basket / negative regulation of ubiquitin protein ligase activity / mitotic spindle assembly checkpoint signaling ...mitotic spindle assembly checkpoint MAD1-MAD2 complex / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of mitotic cell cycle spindle assembly checkpoint / establishment of centrosome localization / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / nuclear pore nuclear basket / negative regulation of ubiquitin protein ligase activity / mitotic spindle assembly checkpoint signaling / mitotic sister chromatid segregation / establishment of mitotic spindle orientation / negative regulation of mitotic cell cycle / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / APC-Cdc20 mediated degradation of Nek2A / RHO GTPases Activate Formins / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / negative regulation of protein catabolic process / mitotic spindle / kinetochore / spindle pole / Separation of Sister Chromatids / cell division / negative regulation of apoptotic process / perinuclear region of cytoplasm / protein homodimerization activity / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Luo, X. / Tang, Z. / Rizo, J. / Yu, H. | ||||||
Citation | Journal: Mol.Cell / Year: 2002 Title: The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20. Authors: Luo, X. / Tang, Z. / Rizo, J. / Yu, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1klq.cif.gz | 74.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1klq.ent.gz | 60.3 KB | Display | PDB format |
PDBx/mmJSON format | 1klq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kl/1klq ftp://data.pdbj.org/pub/pdb/validation_reports/kl/1klq | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 22562.725 Da / Num. of mol.: 1 / Fragment: MISSING N-TERMINAL 10 RESIDUES Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pQE-30 / Production host: Escherichia coli (E. coli) / Strain (production host): M15[pREP4] / References: UniProt: Q13257 |
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#2: Protein/peptide | Mass: 1451.604 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: This sequence is identified using phage display |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: The structures are based on a total of 3124 restraints, 2535 are NOE-derived distance constraints, 363 dihedral angle restraints,226 distance restraints from hydrogen bonds. | ||||||||||||
NMR representative | Selection criteria: the best representative conformer | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 1 |