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Yorodumi- PDB-1zy3: Structural model of complex of Bcl-w protein with Bid BH3-peptide -
+Open data
-Basic information
Entry | Database: PDB / ID: 1zy3 | ||||||
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Title | Structural model of complex of Bcl-w protein with Bid BH3-peptide | ||||||
Components |
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Keywords | APOPTOSIS / Bcl-w / BH3-peptide | ||||||
Function / homology | Function and homology information negative regulation of mitochondrial membrane permeability / cysteine-type endopeptidase regulator activity involved in apoptotic process / mitochondrial outer membrane permeabilization / Activation, translocation and oligomerization of BAX / Activation and oligomerization of BAK protein / Sertoli cell proliferation / Activation, myristolyation of BID and translocation to mitochondria / BH domain binding / positive regulation of fibroblast apoptotic process / BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members ...negative regulation of mitochondrial membrane permeability / cysteine-type endopeptidase regulator activity involved in apoptotic process / mitochondrial outer membrane permeabilization / Activation, translocation and oligomerization of BAX / Activation and oligomerization of BAK protein / Sertoli cell proliferation / Activation, myristolyation of BID and translocation to mitochondria / BH domain binding / positive regulation of fibroblast apoptotic process / BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / protein targeting to mitochondrion / regulation of epithelial cell proliferation / establishment of protein localization to membrane / death receptor binding / positive regulation of extrinsic apoptotic signaling pathway / positive regulation of mitochondrial membrane potential / Bcl-2 family protein complex / regulation of T cell proliferation / hepatocyte apoptotic process / negative regulation of release of cytochrome c from mitochondria / regulation of G1/S transition of mitotic cell cycle / apoptotic mitochondrial changes / positive regulation of release of cytochrome c from mitochondria / TP53 Regulates Transcription of Genes Involved in Cytochrome C Release / mitochondrial ATP synthesis coupled electron transport / cellular response to glycine / extrinsic apoptotic signaling pathway via death domain receptors / Activation of BAD and translocation to mitochondria / signal transduction in response to DNA damage / supramolecular fiber organization / negative regulation of intrinsic apoptotic signaling pathway / positive regulation of intrinsic apoptotic signaling pathway / extrinsic apoptotic signaling pathway in absence of ligand / release of cytochrome c from mitochondria / cellular response to estradiol stimulus / response to ischemia / positive regulation of protein-containing complex assembly / cellular response to amyloid-beta / intrinsic apoptotic signaling pathway in response to DNA damage / disordered domain specific binding / spermatogenesis / protein-containing complex assembly / regulation of apoptotic process / neuron apoptotic process / mitochondrial outer membrane / positive regulation of apoptotic process / protein heterodimerization activity / ubiquitin protein ligase binding / protein-containing complex binding / negative regulation of apoptotic process / protein homodimerization activity / mitochondrion / identical protein binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / Rigid body docking, semi-flexible simulated annealing, refinement using explicit water | ||||||
Authors | Denisov, A.Y. / Gehring, K. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: Structural Model of the BCL-w-BID Peptide Complex and Its Interactions with Phospholipid Micelles. Authors: Denisov, A.Y. / Chen, G. / Sprules, T. / Moldoveanu, T. / Beauparlant, P. / Gehring, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zy3.cif.gz | 566.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zy3.ent.gz | 472.2 KB | Display | PDB format |
PDBx/mmJSON format | 1zy3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1zy3_validation.pdf.gz | 354.7 KB | Display | wwPDB validaton report |
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Full document | 1zy3_full_validation.pdf.gz | 477.3 KB | Display | |
Data in XML | 1zy3_validation.xml.gz | 36.5 KB | Display | |
Data in CIF | 1zy3_validation.cif.gz | 48.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zy/1zy3 ftp://data.pdbj.org/pub/pdb/validation_reports/zy/1zy3 | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 19659.885 Da / Num. of mol.: 1 / Fragment: residues 2-171 / Mutation: P116V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET-29b+ / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q92843 |
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#2: Protein/peptide | Mass: 2241.615 Da / Num. of mol.: 1 / Mutation: R203K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX-6P-1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P55957 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This model structure was obtained using ambigous chemical shift perturbation constraints, NOE distances and hydrogen bonds |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 10 mM NaCl / pH: 7.0 / Pressure: 1 atm / 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: Rigid body docking, semi-flexible simulated annealing, refinement using explicit water Software ordinal: 1 Details: 200 conformers were obtained in the rigid body docking and 100 best conformers were selected for semi-flexible simulated annealing following by refinement | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |