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Yorodumi- PDB-2mpx: Three-dimensional structure of CAP-GLY DOMAIN ASSEMBLED ON MICROT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2mpx | ||||||
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Title | Three-dimensional structure of CAP-GLY DOMAIN ASSEMBLED ON MICROTUBULES DETERMINED BY MAS NMR SPECTROSCOPY | ||||||
Components | Dynactin subunit 1 | ||||||
Keywords | MOTOR PROTEIN / structure of CAP-Gly domain assembled on microtubules | ||||||
Function / homology | Function and homology information COPI-independent Golgi-to-ER retrograde traffic / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / Regulation of PLK1 Activity at G2/M Transition / positive regulation of neuromuscular junction development / centriolar subdistal appendage ...COPI-independent Golgi-to-ER retrograde traffic / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / Regulation of PLK1 Activity at G2/M Transition / positive regulation of neuromuscular junction development / centriolar subdistal appendage / COPI-mediated anterograde transport / cell cortex region / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / centriole-centriole cohesion / ventral spinal cord development / microtubule anchoring at centrosome / MHC class II antigen presentation / melanosome transport / retromer complex / nuclear membrane disassembly / microtubule plus-end / positive regulation of microtubule nucleation / positive regulation of intracellular protein transport / cytoplasmic dynein complex / non-motile cilium assembly / retrograde transport, endosome to Golgi / nuclear migration / microtubule associated complex / motor behavior / neuromuscular process / neuromuscular junction development / cell leading edge / establishment of mitotic spindle orientation / cytoplasmic microtubule organization / regulation of mitotic spindle organization / positive regulation of microtubule polymerization / neuron projection maintenance / centriole / tubulin binding / ciliary basal body / spindle / kinetochore / spindle pole / neuron cellular homeostasis / nuclear envelope / cell cortex / microtubule binding / microtubule / molecular adaptor activity / neuron projection / cell division / axon / centrosome / neuronal cell body / protein kinase binding / protein-containing complex / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLID-STATE NMR / simulated annealing, torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Yan, S. / Hou, G. / Zhang, H. / Polenova, T. / Williams, J.C. | ||||||
Citation | Journal: To be Published Title: THREE-DIMENSIONAL STRUCTURE of CAP-GLY DOMAIN ASSEMBLED ON MICROTUBULES DETERMINED BY MAS NMR SPECTROSCOPY Authors: Yan, S. / Polenova, T. / Williams, J. / Zhang, H. / Hou, G. / Ahmed, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mpx.cif.gz | 214.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mpx.ent.gz | 180.3 KB | Display | PDB format |
PDBx/mmJSON format | 2mpx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mp/2mpx ftp://data.pdbj.org/pub/pdb/validation_reports/mp/2mpx | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7572.622 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Dctn1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P28023 |
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-Experimental details
-Experiment
Experiment | Method: SOLID-STATE 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: 0.0737 / pH: 6.0 / Pressure: ambient / Temperature: 244 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 850 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR constraints | Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 56 / Protein psi angle constraints total count: 56 | ||||||||||||||||||||||||||||
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: 10 |