+Open data
-Basic information
Entry | Database: PDB / ID: 2l39 | ||||||
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Title | Mouse prion protein fragment 121-231 AT 37 C | ||||||
Components | Major prion protein | ||||||
Keywords | MEMBRANE PROTEIN / prion / conformational exchange | ||||||
Function / homology | Function and homology information Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / 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 / negative regulation of interleukin-17 production ...Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / 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 / negative regulation of interleukin-17 production / negative regulation of dendritic spine maintenance / type 5 metabotropic glutamate receptor binding / cupric ion binding / nucleobase-containing compound metabolic process / response to copper ion / negative regulation of calcineurin-NFAT signaling cascade / negative regulation of interleukin-2 production / negative regulation of T cell receptor signaling pathway / activation of protein kinase activity / 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 / side of membrane / response to cadmium ion / regulation of peptidyl-tyrosine phosphorylation / inclusion body / cellular response to copper ion / neuron projection maintenance / protein sequestering activity / 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 / regulation of protein localization / 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 / microtubule binding / nuclear membrane / protease binding / response to oxidative stress / mitochondrial outer membrane / transmembrane transporter binding / postsynaptic density / molecular adaptor activity / learning or memory / membrane raft / copper ion binding / intracellular membrane-bounded organelle / dendrite / protein-containing complex binding / negative regulation of apoptotic process / Golgi apparatus / cell surface / endoplasmic reticulum / membrane / identical protein binding / metal ion binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | fewest violations, model 1 | ||||||
Authors | Christen, B. / Damberger, F.F. / Perez, D.R. / Hornemann, S. / Wuthrich, K. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2011 Title: Cellular prion protein conformation and function. Authors: Damberger, F.F. / Christen, B. / Perez, D.R. / Hornemann, S. / Wuthrich, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l39.cif.gz | 697.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l39.ent.gz | 587.5 KB | Display | PDB format |
PDBx/mmJSON format | 2l39.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l3/2l39 ftp://data.pdbj.org/pub/pdb/validation_reports/l3/2l39 | 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: 13408.877 Da / Num. of mol.: 1 / Fragment: UNP residues 120-231 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Prnp, RP23-401J24.1-001 / Production host: Escherichia coli (E. coli) / References: UniProt: Q4FJQ7, UniProt: P04925*PLUS |
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Sequence details | RESIDUES GLY A 119 AND SER A 120 ARE LEFT OVER FROM THE THROMBIN CLEAVAGE OF THE HIS TAG |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Additional HN/N signals from the beta 2-alpha 2 loop of the mouse prion protein fragment 121-231 are visible at 37C allowing the identification of additional NOE constraints which lead to a ...Details: Additional HN/N signals from the beta 2-alpha 2 loop of the mouse prion protein fragment 121-231 are visible at 37C allowing the identification of additional NOE constraints which lead to a defined conformation for the loop. | ||||||||||||||||
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NMR experiment |
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NMR details | Text: Two 13C-resolved [1H,1H]-NOESY spectra were obtained with the 13C carrier and spectral width optimized for aliphatic and aromatic 13C resonances respectively. |
-Sample preparation
Details | Contents: 1.6 mM [U-99% 13C; U-99% 15N] entity-1, 10 mM [U-2H] sodium acetate-2, 0.02 % sodium azide-3, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.01 / pH: 4.5 / Pressure: ambient / Temperature: 310.2 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 120 / Conformers submitted total number: 20 / Representative conformer: 1 |