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- SASDED2: Polyglutamine tract-binding protein 1 (PQBP-1) (Polyglutamine-bin... -

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Basic information

Entry
Database: SASBDB / ID: SASDED2
SamplePolyglutamine tract-binding protein 1 (PQBP-1)
  • Polyglutamine-binding protein 1 (protein), PQBP-1, Homo sapiens
Function / homology
Function and homology information


neuronal ribonucleoprotein granule / alternative mRNA splicing, via spliceosome / regulation of dendrite morphogenesis / cellular response to exogenous dsRNA / regulation of RNA splicing / positive regulation of type I interferon production / ribonucleoprotein complex binding / positive regulation of defense response to virus by host / activation of innate immune response / mRNA Splicing - Major Pathway ...neuronal ribonucleoprotein granule / alternative mRNA splicing, via spliceosome / regulation of dendrite morphogenesis / cellular response to exogenous dsRNA / regulation of RNA splicing / positive regulation of type I interferon production / ribonucleoprotein complex binding / positive regulation of defense response to virus by host / activation of innate immune response / mRNA Splicing - Major Pathway / cytoplasmic stress granule / neuron projection development / double-stranded DNA binding / defense response to virus / transcription coactivator activity / nuclear body / nuclear speck / innate immune response / regulation of DNA-templated transcription / DNA binding / nucleoplasm / nucleus / cytoplasm
Similarity search - Function
WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain
Similarity search - Domain/homology
Polyglutamine-binding protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationJournal: Biophys J / Year: 2012
Title: Solution model of the intrinsically disordered polyglutamine tract-binding protein-1.
Authors: Martin Rees / Christian Gorba / Cesira de Chiara / Tam T T Bui / Mitla Garcia-Maya / Alex F Drake / Hitoshi Okazawa / Annalisa Pastore / Dmitri Svergun / Yu Wai Chen /
Abstract: Polyglutamine tract-binding protein-1 (PQBP-1) is a 265-residue nuclear protein that is involved in transcriptional regulation. In addition to its role in the molecular pathology of the polyglutamine ...Polyglutamine tract-binding protein-1 (PQBP-1) is a 265-residue nuclear protein that is involved in transcriptional regulation. In addition to its role in the molecular pathology of the polyglutamine expansion diseases, mutations of the protein are associated with X-linked mental retardation. PQBP-1 binds specifically to glutamine repeat sequences and proline-rich regions, and interacts with RNA polymerase II and the spliceosomal protein U5-15kD. In this work, we obtained a biophysical characterization of this protein by employing complementary structural methods. PQBP-1 is shown to be a moderately compact but largely disordered molecule with an elongated shape, having a Stokes radius of 3.7 nm and a maximum molecular dimension of 13 nm. The protein is monomeric in solution, has residual β-structure, and is in a premolten globule state that is unaffected by natural osmolytes. Using small-angle x-ray scattering data, we were able to generate a low-resolution, three-dimensional model of PQBP-1.
Contact author
  • Yu Wai Chen (King's College London)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #2194
Type: dummy / Software: (1.1.0 r980) / Radius of dummy atoms: 2.70 A / Chi-square value: 1.018081 / P-value: 0.058031
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Polyglutamine tract-binding protein 1 (PQBP-1) / Specimen concentration: 7.00-13.00
BufferName: 20 mM Tris, 150 mM NaCl, 1mM DTT, / pH: 7
Entity #1201Name: PQBP-1 / Type: protein / Description: Polyglutamine-binding protein 1 / Formula weight: 30.626 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: O60828
Sequence: GPMPLPVALQ TRLAKRGILK HLEPEPEEEI IAEDYDDDPV DYEATRLEGL PPSWYKVFDP SCGLPYYWNA DTDLVSWLSP HDPNSVVTKS AKKLRSSNAD AEEKLDRSHD KSDRGHDKSD RSHEKLDRGH DKSDRGHDKS DRDRERGYDK VDRERERDRE RDRDRGYDKA ...Sequence:
GPMPLPVALQ TRLAKRGILK HLEPEPEEEI IAEDYDDDPV DYEATRLEGL PPSWYKVFDP SCGLPYYWNA DTDLVSWLSP HDPNSVVTKS AKKLRSSNAD AEEKLDRSHD KSDRGHDKSD RSHEKLDRGH DKSDRGHDKS DRDRERGYDK VDRERERDRE RDRDRGYDKA DREEGKERRH HRREELAPYP KSKKAVSRKD EELDPMDPSS YSDAPRGTWS TGLPKRNEAK TGADTTAAGP LFQQRPYPSP GAVLRANAEA SRTKQQD

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Experimental information

BeamInstrument name: DORIS III EMBL X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm
DetectorName: Pilatus 1M-W / Pixsize x: 0.172 mm
Scan
Title: Polyglutamine tract-binding protein 1 (PQBP-1) / Measurement date: Nov 18, 2009 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 15 sec. / Number of frames: 8 / Unit: 1/nm /
MinMax
Q0.0775 6.2077
Distance distribution function P(R)
Sofotware P(R): GNOM 4.5a / Number of points: 500 /
MinMax
Q0.07879 2.741
P(R) point1 500
R0 13
Result
Type of curve: merged
ExperimentalStandardStandard errorPorod
MW30.6 kDa30 kDa3 35 kDa
Volume---51 nm3

P(R)GuinierGuinier error
Forward scattering, I040.75 40.49 -
Radius of gyration, Rg3.82 nm3.72 nm0.2

MinMax
D-13
Guinier point30 97

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