[English] 日本語
Yorodumi- SASDCJ2: Solution structure of recombinant prion protein (89–230) in compl... -
+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDCJ2 |
---|---|
Sample | Solution structure of recombinant prion protein (89–230) in complex with Fab-P
|
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 T cell receptor signaling pathway / negative regulation of interleukin-2 production / activation of protein kinase activity / cuprous ion binding / negative regulation of amyloid-beta formation / negative regulation of activated T cell proliferation / regulation of peptidyl-tyrosine phosphorylation / response to amyloid-beta / negative regulation of type II interferon production / negative regulation of long-term synaptic potentiation / intracellular copper ion homeostasis / positive regulation of protein targeting to membrane / side of membrane / response to cadmium ion / inclusion body / cellular response to copper ion / neuron projection maintenance / positive regulation of calcium-mediated signaling / positive regulation of protein localization to plasma membrane / molecular condensate scaffold activity / negative regulation of protein phosphorylation / molecular function activator activity / protein destabilization / protein homooligomerization / negative regulation of DNA-binding transcription factor activity / terminal bouton / cellular response to xenobiotic stimulus / cellular response to amyloid-beta / positive regulation of peptidyl-tyrosine phosphorylation / regulation of protein localization / positive regulation of neuron apoptotic process / signaling receptor activity / amyloid-beta binding / protein-folding chaperone binding / nuclear membrane / microtubule binding / protease binding / response to oxidative stress / transmembrane transporter binding / learning or memory / molecular adaptor activity / postsynaptic density / membrane raft / copper ion binding / dendrite / negative regulation of apoptotic process / protein-containing complex binding / cell surface / Golgi apparatus / endoplasmic reticulum / identical protein binding / membrane / metal ion binding / plasma membrane / cytosol Similarity search - Function |
Biological species | Mus musculus (house mouse) Homo sapiens (human) |
Citation | Journal: Biophys J / Year: 2015 Title: Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Authors: Lester Carter / Seung Joong Kim / Dina Schneidman-Duhovny / Jan Stöhr / Guillaume Poncet-Montange / Thomas M Weiss / Hiro Tsuruta / Stanley B Prusiner / Andrej Sali / Abstract: Aberrant self-assembly, induced by structural misfolding of the prion proteins, leads to a number of neurodegenerative disorders. In particular, misfolding of the mostly α-helical cellular prion ...Aberrant self-assembly, induced by structural misfolding of the prion proteins, leads to a number of neurodegenerative disorders. In particular, misfolding of the mostly α-helical cellular prion protein (PrP(C)) into a β-sheet-rich disease-causing isoform (PrP(Sc)) is the key molecular event in the formation of PrP(Sc) aggregates. The molecular mechanisms underlying the PrP(C)-to-PrP(Sc) conversion and subsequent aggregation remain to be elucidated. However, in persistently prion-infected cell-culture models, it was shown that treatment with monoclonal antibodies against defined regions of the prion protein (PrP) led to the clearing of PrP(Sc) in cultured cells. To gain more insight into this process, we characterized PrP-antibody complexes in solution using a fast protein liquid chromatography coupled with small-angle x-ray scattering (FPLC-SAXS) procedure. High-quality SAXS data were collected for full-length recombinant mouse PrP [denoted recPrP(23-230)] and N-terminally truncated recPrP(89-230), as well as their complexes with each of two Fab fragments (HuM-P and HuM-R1), which recognize N- and C-terminal epitopes of PrP, respectively. In-line measurements by fast protein liquid chromatography coupled with SAXS minimized data artifacts caused by a non-monodispersed sample, allowing structural analysis of PrP alone and in complex with Fab antibodies. The resulting structural models suggest two mechanisms for how these Fabs may prevent the conversion of PrP(C) into PrP(Sc). |
Contact author |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Data source
SASBDB page | SASDCJ2 |
---|
-Related structure data
Similar structure data |
---|
-External links
Related items in Molecule of the Month |
---|
-Models
Model #1168 | Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 1.27153004943 / P-value: 0.058000 Search similar-shape structures of this assembly by Omokage search (details) |
---|---|
Model #1169 | Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 1.27153004943 / P-value: 0.058000 Search similar-shape structures of this assembly by Omokage search (details) |
Model #1167 | Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 4.55590410686 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: Solution structure of recombinant prion protein (89–230) in complex with Fab-P Specimen concentration: 1.00-3.70 / Entity id: 606 / 607 |
---|---|
Buffer | Name: sodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl) pH: 5.1 |
Entity #606 | Name: prion / Type: protein / Description: Major prion protein / Formula weight: 22.932 / Num. of mol.: 1 / Source: Mus musculus / References: UniProt: P04925 Sequence: KKRPKPGGWN TGGSRYPGQG SPGGNRYPPQ GGTWGQPHGG GWGQPHGGSW GQPHGGSWGQ PHGGGWGQGG GTHNQWNKPS KPKTNLKHVA GAAAAGAVVG GLGGYMLGSA MSRPMIHFGN DWEDRYYREN MYRYPNQVYY RPVDQYSNQN NFVHDCVNIT IKQHTVTTTT ...Sequence: KKRPKPGGWN TGGSRYPGQG SPGGNRYPPQ GGTWGQPHGG GWGQPHGGSW GQPHGGSWGQ PHGGGWGQGG GTHNQWNKPS KPKTNLKHVA GAAAAGAVVG GLGGYMLGSA MSRPMIHFGN DWEDRYYREN MYRYPNQVYY RPVDQYSNQN NFVHDCVNIT IKQHTVTTTT KGENFTETDV KMMERVVEQM CVTQYQKESQ AYYDGRRS |
Entity #607 | Name: Fab-P / Type: protein / Description: P-Clone Fab, Chimera / Formula weight: 47.386 / Num. of mol.: 1 / Source: Homo sapiens Sequence: ATQAYAELVM TQTPSSLSAS LGERVSLTCR ASQDIGNNLN WIQQKPDGTI KRLIYATSSL DSGVPKRFSG SRSGSDYSLT ISSLESEDFA DYYCLQHDTF PLTFGGGTKL EIKRTVAAPS VFIFPPSDEQ LKSGTASVVC LLNNFYPREA KVQWKVDNAL QSGNSQESVT ...Sequence: ATQAYAELVM TQTPSSLSAS LGERVSLTCR ASQDIGNNLN WIQQKPDGTI KRLIYATSSL DSGVPKRFSG SRSGSDYSLT ISSLESEDFA DYYCLQHDTF PLTFGGGTKL EIKRTVAAPS VFIFPPSDEQ LKSGTASVVC LLNNFYPREA KVQWKVDNAL QSGNSQESVT EQDSKDSTYS LSSTLTLSKA DYEKHKVYAC EVTHQGLSSP VTKSFNRAYA EVQLLEQSGA ELVKPGASVK LSCTASGFNI EDSYIHWVKQ RPEQGLEWIG RIDPEDGETK YAPKFQGKAT ITADTSSNTA YLHLRRLTSE DTAIYYCGRG AYYIKEDFWG QGTTLTVSSA STKGPSVFPL APSSKAGGTA ALGCLVKDYF PEPVTVSWNS GALTSGVHTF PAVLQSSGLY SLSSVVTVPS SSLGTQTYIC NVNHKPSNTK VDKKVEPA |
-Experimental information
Beam | Instrument name: Stanford Synchrotron Radiation Lightsource (SSRL) BL4-2 City: Stanford, CA / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.113 Å / Dist. spec. to detc.: 1.7 mm | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Detector | Name: Rayonix MX225-HE | ||||||||||||||||||||||||||||||||||||
Scan | Title: Solution structure of recombinant prion protein (89–230) in complex with Fab-P Measurement date: Dec 5, 2013 / Storage temperature: 4 °C / Cell temperature: 9.8 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/A /
| ||||||||||||||||||||||||||||||||||||
Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 498 /
| ||||||||||||||||||||||||||||||||||||
Result | Type of curve: merged /
|