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Yorodumi- PDB-1re6: Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptot... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1re6 | ||||||
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Title | Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands | ||||||
Components | dynein light chain 2 | ||||||
Keywords | CONTRACTILE PROTEIN / dynein light chain / apoptosis / dimer | ||||||
Function / homology | Function and homology information Activation of BMF and translocation to mitochondria / Intraflagellar transport / Macroautophagy / myosin V complex / COPI-independent Golgi-to-ER retrograde traffic / 9+0 non-motile cilium / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / Aggrephagy ...Activation of BMF and translocation to mitochondria / Intraflagellar transport / Macroautophagy / myosin V complex / COPI-independent Golgi-to-ER retrograde traffic / 9+0 non-motile cilium / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / Aggrephagy / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / RHO GTPases Activate Formins / Separation of Sister Chromatids / MHC class II antigen presentation / cytoplasmic dynein complex / dynein intermediate chain binding / microtubule-based process / postsynapse / scaffold protein binding / microtubule / postsynaptic density / cytoskeleton / centrosome / glutamatergic synapse / protein-containing complex binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics | ||||||
Authors | Day, C.L. / Puthalakath, H. / Skea, G. / Strasser, A. / Barsukov, I. / Lian, L.Y. / Huang, D.C. / Hinds, M.G. | ||||||
Citation | Journal: Biochem.J. / Year: 2004 Title: Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. Authors: Day, C.L. / Puthalakath, H. / Skea, G. / Strasser, A. / Barsukov, I. / Lian, L.Y. / Huang, D.C. / Hinds, M.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1re6.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1re6.ent.gz | 1004.3 KB | Display | PDB format |
PDBx/mmJSON format | 1re6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/re/1re6 ftp://data.pdbj.org/pub/pdb/validation_reports/re/1re6 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10776.303 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: DLC2 / Plasmid: PGEX6P-3 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: GenBank: 18087731, UniProt: Q9D0M5*PLUS |
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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 STANDARD 2D AND 3D HETERONUCLEAR TECHNIQUES |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-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: distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics Software ordinal: 1 Details: the structures are based on a total of 1602 restraints, 1417 are NOE derived distance constraints,99 are interprotomer distance constraints, 127 are dihedral angle restraints and 29 hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy,target function Conformers calculated total number: 256 / Conformers submitted total number: 20 |