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- PDB-1s2h: The Mad2 spindle checkpoint protein possesses two distinct native... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1s2h | ||||||
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Title | The Mad2 spindle checkpoint protein possesses two distinct natively folded states | ||||||
![]() | Mitotic spindle assembly checkpoint protein MAD2A | ||||||
![]() | CELL CYCLE / Mad2 / spindle checkpoint protein | ||||||
Function / homology | ![]() 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 / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Luo, X. / Tang, Z. / Xia, G. / Wassmann, K. / Matsumoto, T. / Rizo, J. / Yu, H. | ||||||
![]() | ![]() Title: The Mad2 spindle checkpoint protein has two distinct natively folded states. Authors: Luo, X. / Tang, Z. / Xia, G. / Wassmann, K. / Matsumoto, T. / Rizo, J. / Yu, H. #1: ![]() Title: Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20 Authors: Luo, X. / Fang, G. / Coldiron, M. / Lin, Y. / Yu, H. / Kirschner, M.W. / Wagner, G. #2: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 77.8 KB | Display | ![]() |
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PDB format | ![]() | 58.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 246 KB | Display | ![]() |
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Full document | ![]() | 245.8 KB | Display | |
Data in XML | ![]() | 7.1 KB | Display | |
Data in CIF | ![]() | 9.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 23504.822 Da / Num. of mol.: 1 / Mutation: R133A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-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. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 0.3M KCl / pH: 6.8 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
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 2866 restraints, 2323 are NOE-derived distance constraints, 339 dihedral angle restraints,204 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: 500 / Conformers submitted total number: 1 |