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Yorodumi- PDB-1fad: DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183 -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fad | ||||||
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Title | DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183 | ||||||
Components | PROTEIN (FADD PROTEIN) | ||||||
Keywords | APOPTOSIS / FADD / DEATH DOMAIN | ||||||
Function / homology | Function and homology information TRAIL signaling / FasL/ CD95L signaling / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / Caspase activation via Death Receptors in the presence of ligand / positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation / TNFR1-induced proapoptotic signaling / TRIF-mediated programmed cell death / negative regulation of activation-induced cell death of T cells ...TRAIL signaling / FasL/ CD95L signaling / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / Caspase activation via Death Receptors in the presence of ligand / positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation / TNFR1-induced proapoptotic signaling / TRIF-mediated programmed cell death / negative regulation of activation-induced cell death of T cells / death effector domain binding / Regulation of TNFR1 signaling / Regulation of necroptotic cell death / CD95 death-inducing signaling complex / ripoptosome / death-inducing signaling complex assembly / TRAIL-activated apoptotic signaling pathway / caspase binding / regulation of necroptotic process / positive regulation of adaptive immune response / positive regulation of macrophage differentiation / necroptotic signaling pathway / negative regulation of necroptotic process / death-inducing signaling complex / receptor serine/threonine kinase binding / tumor necrosis factor receptor binding / positive regulation of innate immune response / positive regulation of type I interferon-mediated signaling pathway / death receptor binding / positive regulation of extrinsic apoptotic signaling pathway / cardiac muscle tissue development / motor neuron apoptotic process / T cell homeostasis / positive regulation of activated T cell proliferation / positive regulation of execution phase of apoptosis / positive regulation of proteolysis / behavioral response to cocaine / T cell differentiation / extrinsic apoptotic signaling pathway via death domain receptors / lymph node development / extrinsic apoptotic signaling pathway in absence of ligand / signaling adaptor activity / spleen development / extrinsic apoptotic signaling pathway / kidney development / thymus development / positive regulation of interleukin-8 production / cellular response to mechanical stimulus / positive regulation of T cell mediated cytotoxicity / positive regulation of type II interferon production / positive regulation of tumor necrosis factor production / T cell differentiation in thymus / cell body / protease binding / defense response to virus / positive regulation of canonical NF-kappaB signal transduction / innate immune response / protein-containing complex binding / apoptotic process / positive regulation of transcription by RNA polymerase II / protein-containing complex / identical protein binding Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMMULATED ANNEALING | ||||||
Authors | Jeong, E.-J. / Bang, S. / Lee, T.H. / Park, Y.-I. / Sim, W.-S. / Kim, K.-S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1999 Title: The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. Authors: Jeong, E.J. / Bang, S. / Lee, T.H. / Park, Y.I. / Sim, W.S. / Kim, K.S. #1: Journal: Mol.Cell.Biol. / Year: 1996 Title: A Mouse Fas-Associated Protein with Homology to the Human Mort1/FADD is Essential for Fas-Induced Apoptosis Authors: Zhang, J. / Winoto, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fad.cif.gz | 676.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fad.ent.gz | 575.7 KB | Display | PDB format |
PDBx/mmJSON format | 1fad.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fad_validation.pdf.gz | 344.7 KB | Display | wwPDB validaton report |
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Full document | 1fad_full_validation.pdf.gz | 487.9 KB | Display | |
Data in XML | 1fad_validation.xml.gz | 38.4 KB | Display | |
Data in CIF | 1fad_validation.cif.gz | 63.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fa/1fad ftp://data.pdbj.org/pub/pdb/validation_reports/fa/1fad | HTTPS FTP |
-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: 11088.693 Da / Num. of mol.: 1 / Fragment: DEATH DOMAIN (RESIDUES 89-183) / Mutation: D96Y Source method: isolated from a genetically manipulated source Details: N-TERMINAL EXTENSION OF GLY-SER-HIS-MET FROM CLONING ARTIFACT. COORDINATES ARE NOT SHOWN FOR ARTIFACT. Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PET15B / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q61160 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: DISTANCE CONSTRAINTS ARE DERIVED FROM THE 3D-13C, 15N-EDITED NOESY. J-COUPLING CONSTANTS FROM HNHA AND 13C CHEMICAL SHIFTS WERE USED AS CONTRAINTS. DURING THE REFINEMENT, DATABASE POTENTIAL WAS USED. |
-Sample preparation
Details | Contents: 2 MM |
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Sample conditions | pH: 4 / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMMULATED ANNEALING / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 50 / Conformers submitted total number: 21 |