+Open data
-Basic information
Entry | Database: PDB / ID: 1fkc | ||||||
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Title | HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231 | ||||||
Components | PRION PROTEINPRNP | ||||||
Keywords | MEMBRANE PROTEIN / three helix / CREUTZFELDT-JAKOB DISEASE / PRION / AGGREGATION | ||||||
Function / homology | Function and homology information positive regulation of glutamate receptor signaling pathway / negative regulation of amyloid precursor protein catabolic process / lamin binding / regulation of glutamate receptor signaling pathway / regulation of calcium ion import across plasma membrane / aspartic-type endopeptidase inhibitor activity / glycosaminoglycan binding / ATP-dependent protein binding / regulation of potassium ion transmembrane transport / NCAM1 interactions ...positive regulation of glutamate receptor signaling pathway / negative regulation of amyloid precursor protein catabolic process / lamin binding / regulation of glutamate receptor signaling pathway / regulation of calcium ion import across plasma membrane / aspartic-type endopeptidase inhibitor activity / glycosaminoglycan binding / ATP-dependent protein binding / regulation of potassium ion transmembrane transport / NCAM1 interactions / negative regulation of interleukin-17 production / negative regulation of dendritic spine maintenance / type 5 metabotropic glutamate receptor binding / cupric ion binding / negative regulation of protein processing / negative regulation of calcineurin-NFAT signaling cascade / dendritic spine maintenance / negative regulation of interleukin-2 production / negative regulation of T cell receptor signaling pathway / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / extrinsic component of membrane / cuprous ion binding / negative regulation of amyloid-beta formation / negative regulation of activated T cell proliferation / response to amyloid-beta / : / negative regulation of type II interferon production / intracellular copper ion homeostasis / negative regulation of long-term synaptic potentiation / positive regulation of protein targeting to membrane / long-term memory / response to cadmium ion / regulation of peptidyl-tyrosine phosphorylation / inclusion body / cellular response to copper ion / neuron projection maintenance / tubulin binding / negative regulation of protein phosphorylation / molecular condensate scaffold activity / molecular function activator activity / positive regulation of protein localization to plasma membrane / protein destabilization / protein homooligomerization / negative regulation of DNA-binding transcription factor activity / terminal bouton / cellular response to amyloid-beta / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of neuron apoptotic process / cellular response to xenobiotic stimulus / signaling receptor activity / amyloid-beta binding / protein-folding chaperone binding / postsynapse / microtubule binding / nuclear membrane / protease binding / response to oxidative stress / transmembrane transporter binding / postsynaptic density / molecular adaptor activity / learning or memory / regulation of cell cycle / membrane raft / copper ion binding / cell cycle / external side of plasma membrane / intracellular membrane-bounded organelle / dendrite / protein-containing complex binding / negative regulation of apoptotic process / Golgi apparatus / cell surface / endoplasmic reticulum / extracellular exosome / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Authors | Zhang, Y. / Swietnicki, W. / Zagorski, M.G. / Surewicz, W.K. / Soennichsen, F.D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2000 Title: Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. Authors: Zhang, Y. / Swietnicki, W. / Zagorski, M.G. / Surewicz, W.K. / Sonnichsen, F.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fkc.cif.gz | 41.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fkc.ent.gz | 32.6 KB | Display | PDB format |
PDBx/mmJSON format | 1fkc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fk/1fkc ftp://data.pdbj.org/pub/pdb/validation_reports/fk/1fkc | HTTPS FTP |
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-Related 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: 16169.063 Da / Num. of mol.: 1 / Fragment: PRP(90-231) / Mutation: E200K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: BRAIN / Organ: BRAIN / Plasmid: PET3 / Production host: Escherichia coli (E. coli) / References: UniProt: P04156 |
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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. |
-Sample preparation
Details | Contents: 0.8 mM E200K(90-231)PrP U-15N,13C; 10mM acetate buffer Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0.00001 / pH: 4.6 / Pressure: 1 atm / Temperature: 299 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: simulated annealing, molecular dynamics / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 60 / Conformers submitted total number: 1 |